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Heat Shock Proteins and Molecular Chaperones
Hsp10
Hsp27
Hsp32
Hsp40
Hsp60
Hsp70
Hsp90
Hsp110
Chaperones
Heat Shock Proteins and Molecular Chaperones
· Antibodies · Proteins · ELISA Kits
02
Heat Shock Proteins and Molecular Chaperones
Heat shock proteins are ubiquitously expressed polypeptides whose
expression increases in response to a variety of different metabolic insults.
Despite their designation, most of the heat shock proteins are constitutively
expressed and perform essential functions. Most notable is their role as
molecular chaperones, facilitating the synthesis and folding of proteins
throughout the cell. In addition, heat shock proteins have been shown to
participate in protein assembly, secretion, trafficking, protein degradation,
and the regulation of transcription factors and protein kinases. Increased
levels of the heat shock proteins after stress plays a central role in cellular
homeostasis.
Assay Designs is committed to providing scientists with reliable tools for
scientific discovery. Our merger in 2005 with Stressgen Bioreagents has
broadened our product offering to include an extensive collection of heat
shock protein related products including ELISA kits, antibodies, recombinant
proteins, and reagents. We are pleased to add the high quality products
generated by over 15 years of Stressgen research into our product line, and
are dedicated to the further development and manufacturing of novel user-
friendly heat shock protein related products. Assay Designs aims to Simplify
Your Science® by offering this guide to the heat shock protein families, and
the products we offer to advance research in this existing field.
Hsp10 ....................................3
Hsp27 ....................................3
Hsp32 ....................................5
Hsp40 and the DnaJ Family ...7
Hsp60 and GroEL ..................9
Hsp70 and DnaK .................11
Hsp90 ..................................13
Hsp110 ................................15
Chaperones & Others .........16
Hsp27 Review .....................20
Hsp70 Review .....................22
Hsp90 Review .....................24
References ..........................26
Species:H: humanM: mouseR: ratB: bovineC: chickenD: drosophilaY: yeast
Applications:WB: western blotIP: immunoprecipitationICC: immunocytochemistryIHC: immunohistochemistryF: flow cytometry
&
Bei Biomol erhalten Sie dieAssay Design- und Stressgen-Produkte:
Bestellen in Deutschland: Biomol GmbHFon: 0800-246 66 51 · Fax: 0800-246 66 [email protected] · www.biomol.deTechnischer Support: [email protected]
Hsp10
Hsp10, also known as Chaperonin 10 (Cpn10), is the ~10
kDa mammalian equivalent of the bacterial GroES gene
product. Hsp10 exists in vivo as an oligomer and interacts
with Hsp60, the mammalian homolog of the bacterial
GroEL protein. Together the Hsp10/Hsp60 chaperonin pre-
sent within mitochondria facilitates the folding of newly
synthesized proteins and may participate in the refolding
of proteins damaged after stress. In plants, a similar chape-
ronin system operates within chloroplasts and is referred
Assay Designs (Stressgen) Products
Cat. No. Product Description Species Application
SPA-110 Hsp10 (Cpn10) Polyclonal Antibody H, M, R, X WB, IP
SPA-210 GroES Polyclonal Antibody E.coli WB, IP
SPP-620 GroES Recombinant Protein E.coli
Official Symbol Name SynonymsEntrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
HSPE1 Heat Shock 10kDa Protein 1 (Chap-eronin 10)
CPN10, GROES, HSP10
3336 Caspase activation, Chaperone binding, Protein folding Broad Mitochondria Chloroplasts
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Application
EKS-500 Hsp27 ELISA Kit H
SPA-796 Hsp20 Polyclonal Antibody H, M, R WB
SPA-801 Hsp25 Polyclonal Antibody M, R WB, IP, ICC, IHC
SPA-803 Hsp27 Polyclonal Antibody H WB, IP, ICC, IHC
SPA-800 Hsp27 Monoclonal Antibody (G3.1) H, M, R WB, IP, ICC, IHC
SPA-525 Hsp27 (phospho-Ser15) Polyclonal Antibody H, M, R WB
SPA-523 Hsp27 (phospho-Ser78) Polyclonal Antibody H, M, R WB, IP
SPA-524 Hsp27 (phospho-Ser82) Polyclonal Antibody H, R WB, IP
905-642 Hsp27 (phospho-Ser82) Monoclonal Antibody H, M, R WB
SPA-800FI Hsp27 Monoclonal Antibody, FITC Conjugate H, M, R F, IF
SPA-800B Hsp27 Monoclonal Antibody, Biotin Conjugate H, M, R
SPA-221 a A Crystallin Polyclonal Antibody B WB, IP
SPA-222 a B Crystallin Monoclonal Antibody H, M, R, B, C WB, ICC, IHC
SPA-223 a B Crystallin Polyclonal Antibody H, M, R, B WB, IP
SPA-224 a A/B Crystallin Polyclonal Antibody B WB
SPA-225 a B Crystallin (phospho-Ser19) Polyclonal Antibody H, M, B WB, IP
SPA-226 a B Crystallin (phospho-Ser45) Polyclonal Antibody H, M, R, B, C, X WB, IP
SPA-227 a B Crystallin (phospho-Ser59) Polyclonal Antibody M, R, B WB, IP
SPA-230 b Crystallin Monoclonal Antibody (3H92) B WB
NSP-510 Hsp25 Recombinant Protein M
SPP-715 Hsp27 Recombinant Protein H
ESP-715 Hsp27 Recombinant Protein - Low Endotoxin H
SPP-226 a A Crystallin Native Protein B
SPP-227 a B Crystallin Native Protein B
SPP-225 a A/B Crystallin Native Protein B
to as the Rubisco-Binding protein. Finally, in bacteria GroEL and
GroES participate in the folding and assembly of numerous pro-
teins.
Hsp27 Hsp27 Review on page 20
Hsp27 (sometimes referred to as
Hsp20, Hsp25, Hsp28 or the low
molecular weight heat shock prote-
in) is homologous to the a Crystallin
proteins. Both families of proteins
are characterized by their oligomeric
structure and are thought to func-
tion as ATP-independent chaperones.
Hsp27 structure/function is thought
to be modulated by phosphorylation
mediated by different protein kinases.
In addition to their chaperone role,
Hsp27 and aB-Crystallin have been
shown to mediate structural integrity
and membrane stability, affecting actin
polymerization, intermediate filament
organization, apoptosis, and invasive
potential. Evidence suggests altered
expression of small heat shock proteins
is implicated in the pathogenesis of
human diseases including cancer, ca-
taracts, neurodegenerative disorders,
and cardiovascular disease.
03
Hsp27 (continued)
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Localization
Human Diseases
CRYAA Crystallin, a A CRYA1, HSPB4 1409 Structural component of eye, Protein Folding
Eye Lens Cytoplasm Cataracts
CRYAB Crystallin, a B CRYA2, HSPB5 1410 Structural component of eye, Protein Folding, Muscle contraction, Muscle development, Protein folding, Receptor mediated signaling, Visual perception
Broad Contrac-tile fibers, Cytoplasm, Nucleus, Plasma membrane
Cataracts, Mul-tiple Sclerosis
HSPB1 Heat Shock 27kDa Protein 1
HSP27, Hsp25 3315 Anti-apoptosis, Cell motility, Protein folding
Broadly Cytoplasm Nucleus, Plasma Membrane
Charcot-Marie-Tooth disease, axonal, type 2F.Neuropathy, distal hereditary motor
HSPB2 Heat Shock 27kDa Protein 2
MKBP 3316 Enzyme Activator, Protein Folding, Somatic Muscle Development
Heart, Skeletal Muscle, Skin
Cytoplasm, Nucleus
HSPB3 Heat Shock 27kDa Protein 3
HSPL27 8988 Protein Folding Muscle
HSPB6 Heat Shock Pro-tein, a-Crystallin-related, B6
Hsp20 126393 Structural component of eye, Protein Folding, Muscle Contraction
Muscle, Ovary Actin cytoskel-eton
HSPB7 Heat Shock 27kDa Protein family, member 7 (cardio-vascular)
cvHSP 27129 Protein Folding, Muscle Contraction Cardiac, Connective, Skeletal
Contractile Fibers
HSPB8 Heat Shock 22kDa Protein 8
H11; E2IG1; HSP22 26353 Kinase Activity, Transferase Activity, Protein Folding
Broadly Cytoplasm, Plasma Mem-brane
Charcot-Marie-Tooth disease type 2L. Hereditary mo-tor neuropathy type II
HSPB9 Heat Shock Pro-tein, a-Crystallin-related, B9
94086 Protein Folding Testes Nucleus, Cyto-plasm
ODF1 Outer dense fiber of sperm tails 1
HSPB10, ODFP, SODF
4956 Structural activity, Cell differentiation, Spermatogenesis
Testes Cytoplasm
Hsp27 (phospho-Ser82) Polyclonal Antibody (Cat. No. SPA-524)Confocal immunofluorescent staining of Hela
cells using Phospho-Hsp (Ser82) Polyclonal Anti-
body (Cat. No. SPA-524; green) (A).
Blue pseudocolor fluorescent dye DRAQ5 was
used to stain cell nuclei (B).
In (C) the two images are overlapped.
A B C
04 H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast
Hsp32 (Heme Qxygenase)
Heme oxygenase or Hsp32 is an es-
sential component in the catabolism
of heme, catalyzing the first step in
the degradation of heme to bilirubin.
Heme oxygenase consists of at least
three isoforms: stress inducible HO-1,
and constitutively expressed HO-2
and HO-3. Induction of HO-1 occurs
in response to heat shock, oxidative
stress, thiol reacting reagents, heavy
metals, inflammatory mediators and
certain growth factors. The majo-
rity of the protein is localized to
the endoplasmic reticulum, but the
protein can also be present at the
plasma membrane and mitochond-
ria. The products produced by heme
oxygenase have important physiolo-
gical effects: carbon monoxide is a
potent vasodilator; biliverdin and its product bilirubin are antioxidants; and the released iron can increase oxidative stress if not
effectively reutilized. Modulation of HO expression may be useful for protection against atherosclerotic disease, oxidative stress,
coronary ischemia, hypertension and certain neurodegenerative diseases.
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
HMOX1 Heme Oxygenase 1 HO-1 3162 Breakdown of heme, protection against oxidative stress, Ion binding, NFkB signaling
Broad Endoplasmic reticulum
HMOX2 Heme Oxygenase 2 HO-2 3163 Breakdown of heme, protection against oxidative stress, Electron carrier, Ion binding
Broad Endoplasmic reticulum
Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-111)Human lung carcinoma tissue was immunohistochemically
stained using Heme-Oxygenase-1 Monoclonal Antibody (clone
HO-1-2) at a dilution of 1:50. Another Heme-Oxygenase-1 mo-
noclonal (clone HO-1-1, Cat. No. OSA-110) (1:50) was negative
for staining the same lung cancer tissue.
Cat. No. Product Description Species Application
EKS-800 HO-1 (Hsp32; Human) ELISA Kit H
EKS-810 HO-1 (Hsp32; Rat) ELISA Kit R
SPA-895 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP, ICC, IHC, F
SPA-896 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP, ICC, IHC
OSA-150 HO-1 (Hsp32) Polyclonal Antibody H, M, R WB, IP
OSA-110 HO-1 (Hsp32) Monoclonal Antibody (HO-1-1) H, M, R WB, F
OSA-111 HO-1 (Hsp32) Monoclonal Antibody (HO-1-2) H, M, R WB, IHC, F
OSA-111FI HO-1 (Hsp32) Monoclonal Antibody-FITC Conjugate H, M, R F, IF
OSA-111B HO-1 (Hsp32) Monoclonal Antibody-Biotin Conjugate H, M, R
OSA-200 HO-2 Polyclonal Antibody H, M, R WB
SPA-897 HO-2 Polyclonal Antibody H, M, R, C WB, IP, ICC
SPP-730 HO-1 (Hsp32) Recombinant Protein R
SPP-732 HO-1 (Hsp32) Recombinant Protein H
NSP-550 HO-2 Recombinant Protein H
05WB: western blot, IP: immunoprecipitation, ICC: immunocytochemistry, IHC: immunohistochemistry, F: flow cytometry
Hsp32 (continued)
Heme-Oxygenase-1 (Hsp32) Monoclonal Antibody (Cat. No. OSA-110)Human lung cancer A2 cells were analyzed by flow cytometry
using isotype control antibody (left) or Heme-Oxygenase-1
Monoclonal Antibody (clone HO-1-1; right) at a final concen-
tration of 10µg/mL.
Heme Oxygenase 1 (Hsp32)Crystal structure of human Heme Oxygenase-1 in complex with
its substrate Heme (Schuller, D.J. et al. 2002).
06
Hsp40 and the DnaJ Family
Mammalian Hsp40, present within the cytosol, is one
of a number of family members closely related to
the DnaJ protein first described in E.coli. Hsp40/DnaJ
family members work in concert with the Hsp70/DnaK
proteins, facilitating the hydrolysis of ATP to ADP and
thereby helping to lock in the binding of the Hsp70
chaperone to its protein substrate. Consequently,
each of the different members of the Hsp70 family in
eukaryotes require a specific DnaJ homolog for their
chaperone activity. More than 20 genes encoding DnaJ-
related proteins have been identified in yeast. In animal cells the Hsp40 family of proteins display a broad tissue distribution with indi-
vidual members present within most intracellular compartments. Assay Designs currently provides both the DnaJ and Hsp40 proteins in
purified form, along with a number of antibodies specific for each protein. New products targeting other members of the DnaJ/Hsp40
family are expected in the near future.
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
DNAJA1 DnaJ (Hsp40) homolog, subfamily A, member 1
DJ-2; DjA1; HDJ2; HSDJ; HSJ2; HSPF4; hDJ-2
3301 Protein binding, Protein folding, LDL receptor binding, Ion binding
Broadly CytoplasmNucleusNucleolusGolgi
DNAJA2 DnaJ (Hsp40) homolog, subfamily A, member 2
CPR3; DJA2; DNAJ; DNJ3; RDJ2; HIRIP4
10294 Protein binding, Ion binding, Cell cycle, Protein Folding
Broadly CytoplasmNucleusMitochondrion
DNAJA3 DnaJ (Hsp40) homolog, subfamily A, member 3
TID1, hTid-1 9093 GTPase activity, Ion Binding, GPCR Signaling, Protein folding, Protein folding, Regulation of apoptosis
Broad Mitochondrion
DNAJA4 DnaJ (Hsp40) homolog, subfamily A, member 4
MST104; MSTP104; PRO1472
55466 Protein binding, Ion binding, Protein folding
Broad
DNAJA5 DnaJ homology subfam-ily A, member 5
GS3 protein 134218 Protein binding, Nucleic acid binding, Ion binding, Protein folding
Broad CytoplasmNucleus
DNAJB1 DnaJ (Hsp40) homolog, subfamily B, member 1
Hdj1; HSPF1; Hsp40 3337 Protein binding, Protein Folding Broad Nucleus
DNAJB2 DnaJ (Hsp40) homolog, subfamily B, member 2
HSJ1; HSPF3 3300 Protein binding, Protein folding Broad CytoplasmNucleus
DNAJB4 DnaJ (Hsp40) homolog, subfamily B, member 4
DjB4; HLJ1; DNAJW 11080 Protein binding, Protein folding Broad
DNAJB5 DnaJ (Hsp40) homolog, subfamily B, member 5
Hsc40 25822 Protein binding, Protein folding Broad
DNAJB6 DnaJ (Hsp40) homolog, subfamily B, member 6
MRJ; HSJ2; HHDJ1; HSJ-2; MSJ-1
10049 Protein binding, Protein folding Broad CytoplasmNucleus
DNAJB7 DnaJ (Hsp40) homolog, subfamily B, member 7
HSC3 150353 Protein Binding, Protein folding Broad
DNAJB8 DnaJ (Hsp40) homolog, subfamily B, member 8
MGC33884 165721 Protein binding, Protein folding
DNAJB9 DnaJ (Hsp40) homolog, subfamily B, member 9
MDG1; ERdj4 4189 Chaperone, Protein folding, activity, Protein binding
Broad CytoplasmEndoplasmic reticulumNucleolus Nucleus
DNAJB11 DnaJ (Hsp40) homolog, subfamily B, member 11
EDJ; ERj3; HEDJ; hDj9; ABBP2; ERdj3; ABBP-2
51726 Protein binding, Protein folding Broad CytoplasmEndoplasmic reticulumNucleus
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Applications
SPA-400 Hsp40 Polyclonal Antibody H, M, R, C, X WB, IP, ICC, IHC
SPA-450 Hsp40 Monoclonal Antibody (2E1) H, M, R WB, IP
SPA-410 DnaJ Polyclonal Antibody E. coli WB, IP
SPP-400 Hsp40 Recombinant Protein H
SPP-640 Active DnaJ Recombinant Protein E. coli
07datasheet: www.biomol.de www.antibodyworld.com
Hsp40 (continued)
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
DNAJB12 DnaJ (Hsp40) homolog, subfamily B, member 12
DJ10 54788 Protein binding, Protein folding Plasma mem-brane
DNAJB13 DnaJ (Hsp40) related, subfamily B, member 13
TSARG5; TSARG6 374407 Protein binding, Apoptosis, Protein folding, Spermatogenesis
Testis
DNAJB14 DnaJ (Hsp40) homolog, subfamily B, member 14
79982 Protein binding, Protein folding
DNAJC1 DnaJ (Hsp40) homolog, subfamily C, member 1
HTJ1; ERdj1; DNAJL1 64215 ATPase activation, Protein folding, Chaperone folding, DNA binding
Endoplasmic reticulumMembraneMicrosomeNucleus
DNAJC2 DnaJ (Hsp40) homolog, subfamily C, member 2
Zrf1; Zrf2; MIDA1 22791 DNA binding, Cell cycle, Protein binding, DNA replication, Protein folding, Transcription
Nucleus
DNAJC3 DnaJ (Hsp40) homolog, subfamily C, member 3
P58; HP58; PRKRI; P58IPK 5611 Protein binding, Protein folding, Kinase inhibitor, Defense
Broad Cytoplasm
DNAJC4 DnaJ (Hsp40) homolog, subfamily C, member 4
HSPF2; MCG18; DANJC4 3338 Protein binding, Protein folding Membrane
DNAJC5 DnaJ (Hsp40) homolog, subfamily C, member 5
CSP 80331 Protein binding, Protein folding Pituitary Gland Membrane
DNAJC5B DnaJ (Hsp40) homolog, subfamily C, member 5 b
CSP-b 85479 Protein binding, Protein folding
DNAJC5G DnaJ (Hsp40) homolog, subfamily C, member 5 g
CSP-g 285126 Protein binding, Protein folding Membrane
DNAJC6 DnaJ (Hsp40) homolog, subfamily C, member 6
DJC6 9829 Protein binding, Signal transduction, Hydrolase activity, Protein folding, Phosphatase activity
Broad Nucleus
DNAJC7 DnaJ (Hsp40) homolog, subfamily C, member 7
TPR2; TTC2; DANJC7 7266 Protein binding, Protein folding
DNAJC8 DnaJ (Hsp40) homolog, subfamily C, member 8
SPF31; HSPC331 22826 Protein binding, Protein folding Nucleolus
DNAJC9 DnaJ (Hsp40) homolog, subfamily C, member 9
JDD1; SB73 23234 Protein binding, Protein folding Broad
DNAJC10 DnaJ (Hsp40) homolog, subfamily C, member 10
JPDI; ERdj5 54431 Protein binding, Redox homeostasis, Protein folding
Broad Endoplasmic Reticulum
DNAJC11 DnaJ (Hsp40) homolog, subfamily C, member 11
55735 Protein binding, Protein folding Mitochondrion
DNAJC12 DnaJ (Hsp40) homolog, subfamily C, member 12
JDP1 56521 Protein binding , Protein folding Broad
DNAJC13 DnaJ (Hsp40) homolog, subfamily C, member 13
RME8 23317 Protein binding, Protein folding Broad Endosome
DNAJC14 DnaJ (Hsp40) homolog, subfamily C, member 14
DNAJ; HDJ3; LIP6 85406 Protein binding, Protein folding Broad Endoplasmic reticulum
DNAJC15 DnaJ (Hsp40) homolog, subfamily C, member 15
MCJ; HSD18; DNAJD1 29103 Protein binding, Protein folding Broad
DNAJC16 DnaJ (Hsp40) homolog, subfamily C, member 16
23341 Protein binding, Protein folding Broad Membrane
DNAJC17 DnaJ (Hsp40) homolog, subfamily C, member 17
55192 RNA binding, Protein folding, Protein binding
DNAJC18 DnaJ (Hsp40) homolog, subfamily C, member 18
202052 Protein binding, Protein folding Membrane
DNAJC19 DnaJ (Hsp40) homolog, subfamily C, member 19
TIM14; TIMM14 131118 Protein binding, Protein folding, Protein transport
MembraneMitochondrion
DNAJC20 HscB iron-sulfur cluster co-chaperone homolog (E. coli)
HSCB, JAC1; HSC20 150274 Chaperone binding, Protein binding, Protein folding
Broad Mitochondrion
HSCB HscB iron-sulfur cluster co-chaperone homolog (E. coli)
DNAJC20 150274
08 H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast
Hsp47 Monoclonal Antibody (Cat. No. SPA-470)Human breast cancer tissue was immunohistochemically
stained using Hsp47 Monoclonal Antibody (clone M16.10A1) at
a dilution of 1:50.
Members of the Hsp60 (eukaryotes) and Gro-
EL (bacterial) family of heat shock proteins
are some of the best characterized molecular
chaperones. Bacterial GroEL, named because of
its essential role in bacteriophage growth, exists
as a large homo-oligomeric complex which re-
cognizes and binds to unfolded polypeptides. In
combination with its particular co-factor (Hsp10
in eukaryotes, GroES in bacteria) the Hsp60/
GroEL proteins bind newly synthesized polypep-
tides and facilitate their folding to the native
state via one or more rounds of ATP hydrolysis.
Mammalian Hsp60 is localized within mito-
chondria, while a related form of the protein
termed Rubisco-binding protein operates within
plant chloroplasts. Finally, within the eukaryotic
cytosol, related proteins referred to as CCT or
TRIC make a hetero-oligomeric structure and
have been shown to similarly bind select protein
substrates and facilitate their folding and/or
higher order assembly. Oftentimes the GroEL/ES
or Hsp60/Hsp10 protein folding machineries
are referred to as the chaperonins. In vitro as
well as in vivo chaperonins, either alone or with
other chaperones and ATP, have been shown to
orchestrate the re-folding of partially denatured
proteins. In addition to their prominent role as
molecular chaperones members of the GroEL
and Hsp60 families have long been recognized as
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Applications
EKS-600 Hsp60 ELISA Kit (measures protein) H
EKS-650 Hsp60 ELISA Kit (measures antibodies) H
SPA-807 Hsp60 Monoclonal Antibody (LK-2) H, M, R, C, Y WB, IHC, F
SPA-806 Hsp60 Monoclonal Antibody (LK-1) H, M, R, C, X WB, IP, F
SPA-829 Hsp60 Monoclonal Antibody (11-13) H, M, R, D WB, IP, IHC, F
SPA-828 Hsp60 Goat Polyclonal Antibody H, M, R, C, X WB, IP
SPA-881 Hsp65 Monoclonal Antibody (3F7) H, M, R, D WB
SPS-870 GroEL Monoclonal Antibody (9A1/2) E. coli WB, IP
SPS-875 GroEL Polyclonal Antibody H, M, R, Y, E. coli WB
SPA-110 Hsp10 (Cpn10) Polyclonal Antibody H,,M, R, X W, IP
SPA-210 GroES Polyclonal Antibody E. coli W, IP
CTA-123 TCP-1a Monoclonal Antibody (23c) M, R W, IP, ICC
CTA-191 TCP-1a Monoclonal Antibody (91a) H, M, R, D, Y WB, IP, F
CTA-202 TCP-1b Monoclonal Antibody H, M, R, C WB
ESP-540 Active Hsp60 Recombinant Protein
(Low Endotoxin)
H
NSP-540 Active Human Hsp60 Recombinant Protein H
ESP-741 Active Mouse Hsp60 Recombinant Protein
(Low Endotoxin)
M
SPP-741 Hsp60 Recombinant Protein M
SPP-742 Hsp60 Recombinant Protein R
NSP-581 Hsp65 Recombinant Protein Mycobacterim
SPP-610 Active GroEL Recombinant Protein E. coli
SPP-620 GroES Recombinant Protein E. coli
Hsp60 and GroEL: the “Chaperonins”
09WB: western blot, IP: immunoprecipitation, ICC: immunocytochemistry, IHC: immunohistochemistry, F: flow cytometry
Hsp60 (continued)
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
HSPD1 Heat Shock 60kDa Protein 1 (chap-eronin)
CPN60; GROEL; HSP60; HSP65; SPG13; HuCHA60
3329 Protein folding, Nucleotide binding, Protein import, Regulation of apoptosis
Broad MitochondrionCytoplasm
Spastic paraplegia
Hsp60 Monoclonal Antibody (Cat. No. SPA-807) Human colon cancer tissue was immunohistochemically stained
using Hsp60 Monoclonal Antibody (clone LK-2) at a dilution of
1:50.
Hsp60 Monoclonal Antibody (Cat. No. SPA-829)Human hepatoma tissue was immunohistochemically stained
using Hsp60 Monoclonal Antibody (clone LK-1) at a dilution
of 1:50. Another Hsp60 monoclonal (clone 11-13, Cat. No.
SPA-806) (1:50) was negative for staining the same hepatoma
tissue.
Hsp60 Monoclonal Antibody (Cat. No. SPA-806)Human hepatoma QGY cells were analyzed by flow cytometry using isotype control antibody (left) or Hsp60 Monoclonal
Antibody (clone LK-1; right) at a final concentration of 10µg/mL.
highly immunogenic proteins and consequently have attracted
much attention from immunologists. Assay Designs offers a
comprehensive panel of both purified chaperonin proteins
isolated from different sources along with antibodies capable
of discerning the different family members.
10
Hsp70 and DnaK Hsp70 Review on page 22
The Hsp70 family of heat shock proteins contains multiple ho-
mologues ranging in size from 66kDa to 78kDa. These proteins
include cognate members which are found within major in-
tracellular compartments, and highly inducible isoforms which
are predominantly cytoplasmic or nuclear in distribution. All
Hsp70 family members contain a highly conserved N-terminal
ATPase domain, as well as a conserved hydrophobic peptide
binding domain (PBD) and more variable a-helical “cap” do-
main. Activation of Hsp70 is coordinated by binding of ATP at
the N-terminus, causing a conformational change that opens
the cap, allowing interaction of the PBD with a wide variety
of client proteins in their unfolded, misfolded, or denatured
state. Hsp70 ATPase activity is influenced by association with
specific co-chaperone molecules, including Hsp40, Hip, Hop,
Hup, Hap, and CHIP. These co-chaperones cooperate with
Hsp70 to fold newly synthesized proteins, re-fold misfolded or
denatured proteins, coordinate trafficking of proteins across
cellular membranes, disassemble clathrin-coated vesicles,
inhibit protein aggregation, and target the degradation of
proteins via the proteasomal pathway. Elevated levels of Hsp70
have been associated with inhibition of apoptosis, and clinical
correlations between Hsp70 expression and poor cellular diffe-
rentiation, increased lymph node metastasis, chemoresistance,
and poor clinical outcome indicate Hsp70 may be of use in the
diagnosis, prognosis, and treatment of human malignancy.
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Applications
EKS-700 Hsp70 ELISA Kit (assay protein) H, M, R
EKS-750 Hsp70 ELISA Kit (assay antibodies) H
EKS-725 Hsp70B’ ELISA Kit (assay protein) H
SPA-810 Hsp70 (Hsp72) Monoclonal Antibody (C92F3A-5) H, M, R, C, D WB, IHC, F
SPA-810FI Hsp70 (Hsp72) Monoclonal Antibody, FITC Conjugate H, M, R, C, D
SPA-810B Hsp70 (Hsp72) Monoclonal Antibody, Biotin Conjugate H, M, R, C, D
SPA-812 Hsp70 (Hsp72) Polyclonal Antibody H, M, R, F WB, IP, ICC, IHC
SPA-811 Hsp70 (Hsp72) Polyclonal Antibody H, M, R WB
SPA-820 Hsp70/Hsc70 Monoclonal Antibody (N27F3-4) H, M, R, C, X WB, F
SPA-822 Hsp70/Hsc70 Monoclonal Antibody (BB70) H, M, R, C, X WB, IHC, F
SPA-757 Hsp70/Hsc70 Polyclonal Antibody H, M, R, C, Y WB, IP
SPA-815 Hsc70 (Hsp73) Rat Monoclonal Antibody (1B5) H, M, R, C WB, IP, ICC, IHC, F
SPA-816 Hsc70 (Hsp73) Polyclonal Antibody H, M, R WB, ICC, IHC
SPA-756 Hsp70B’ Polyclonal Antibody H WB, IP
SPA-754 Hsp70B’ Monoclonal Antibody (175f) H WB
SPA-766 Hip Polyclonal Antibody H, M, R, B WB
SRA-1500 HOP (p60) Monoclonal Antibody (DS14F5) H, M, R, C, X WB, IP
SPS-825 Grp75 Monoclonal Antibody (30A5) H, M, R, C, D, X WB, IHC
SPA-826 Grp78 (BiP) Polyclonal Antibody M, R, X WB, IP, ICC, IHC
NSP-555 Active Hsp70 (Hsp72) Recombinant Protein H
ESP-555 Active Hsp70 Recombinant Protein (Low Endotoxin) H
SPP-758 Active Hsp70 (Hsp72) Recombinant Protein R
SPP-751 Active Hsc70 (Hsp73) Recombinant Protein B
SPP-752 Active Hsc70 (Hsp73) Recombinant Protein,
ATPase fragment
B
ESP-502 Active Hsp70-A2 Recombinant Protein
(Low Endotoxin)
M
SPP-762 Hsp70B’ Recombinant Protein H
SPP-767 Hip Recombinant Protein R
SRP-1510 HOP (p60) Recombinant Protein H
SPP-765 Grp78 (BiP) Recombinant Protein Hamster
11datasheet: www.biomol.de www.antibodyworld.com
Hsp70 (continued)
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
HSPA1A Heat Shock 70kDa Protein 1A
HSP72, HSPA1, HSPA1B, HSP70-1
3303 Nucleotide binding, Protein folding
Broadly Cytoplasm, Nucleolus
Alzheimer’s, Ankylosing spondylitis, Asthma, Chronic obstructive pulmo-nary , Multiple sclerosis, Parkinson’s disease, Restenosis, Schizophrenia, Tuberculosis
HSPA1B Heat Shock 70kDa Protein 1B
HSP70-2 3304 Nucleotide binding, Protien folding, Regulation of apoptosis
Broad? Cytoplasm, Endoplasmic reticulum, Mitochondrion Nucleus
Asthma, Alzheimer’s, Obesity, Chronic obstructive pulmonary, Crohn’s disease, Diabetes (type 1 & 2), Hypothyroid-ism, Multiple, Pancreatitis, Parkinson’s disease, Schizophrenia, Sclerosis, Restenosis
HSPA1L Heat Shock 70kDa Protein 1-like
Hum70t, HSP70-HOM
3305 Nucleotide binding, DNA repair, Protein fold-ing, Telomere maintenance
Broad? Cytoplasm, Nucleus
Chronic obstructive pulmonary disease, Graft vs. Host disease, Hypothyroidism, Multiple sclerosis, Parkinson’s disease, Restenosis, Schizophrenia, Septic shock, Storke
HSPA2 Heat Shock 70kDa Protein 2
3306 Nucleotide binding, Protein folding, Spermatogenesis
Broad Nucleus, Cytoplasm, Nucleolus
Alzheimer’s, Crohn’s, Sepsis
HSPA4 Heat Shock 70kDa Protein 4
RY, APG-2, Hsp70, Hsp70RY, HS24/P52
3308 Nucleotide binding, Protein folding
Broad Cytoplasm Preterm delivery, Carotid Plaques
HSPA5 Heat Shock 70kDa Protein 5 (glucose-regu-lated protein, 78kDa)
BIP, MIF2, GRP78
3309 Nucleotide binding, Apoptosis, Caspase regu-lation, Protein binding, Ribosome binding
Broad Endoplasmic Reticulum, Plasma Mem-brane, Cytoplasm, Nucleolus,
Bipolar disease, Schizophrenia
HSPA6 Heat Shock 70kDa Protein 6 (HSP70B’)
3310 Nucleotide binding, Protein folding
Nucleus
HSPA7 Heat Shock 70kDa Protein 7 (HSP70B)
HSP70B 3311 Nucleotide binding, rotein folding
HSPA8 Heat Shock 70kDa Protein 8
LAP1, HSC54, HSC70, HSC71, HSP71, HSP73, NIP71, HSPA10
3312 Nucleotide binding, Protein folding, ATPase activity
Broad Cytoplasm, Nucleus
Cystic Fibrosis, Lung cancer
HSPA9 Heat Shock 70kDa Protein 9 (Mortalin)
CSA, MOT, MOT2, GRP75, HSPA9, PBP74, Mot-2
3313 Nucleotide binding, Protein folding, Regulation of apoptosis
CytoplasmMitochondria
HSPA14 Heat Shock 70kDa Protein 14
HSP70-4; HSP70L1
51182
Hsp70Substrate binding domain of Hsp70 in complex with a substrate peptide.
Science (1996) 272(5268):1606-1614.
Hsp70 Monoclonal Antibody (Cat. No. SPA-810) Human colon cancer tissue was immunohisto-
chemically stained using Hsp70 Monoclonal
Antibody (clone C92F3A-5) at a dilution of 1:50.
12 H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast
Hsp90 Hsp90 Review on page 24
The 90kDa molecular chaperone family comprises several
proteins including the 90 kDa heat shock protein Hsp90 and
the 94kDa glucose-regulated protein grp94, which are major
molecular chaperones of the cytosol and endoplasmic reticu-
lum. In mammalian cells there are at least two Hsp90 isoforms,
Hsp90a and Hsp90b, which are encoded by separate genes. All
known members of the Hsp90 protein family are highly conser-
ved, especially in the N-terminal and C-terminal regions which
contain independent chaperone sites with different client
protein specificity. Hsp90 is part of the cell’s network of cha-
perones that regulate protein folding and assembly, requiring
both ATP and co-chaperones (e.g. Hsp70, Hsp40, Hip/Hop, p23,
and Aha1) for function. Inhibition of the Hsp90 protein folding
machinery targets client proteins for ubiquitin-mediated
proteolysis. Hsp90 is also a necessary component of fundamen-
tal cellular processes such as hormone signaling, cell growth,
and differentiation through its binding of client proteins such
as ErbB2/Her-2, Akt, Raf, CDK1, and CDK4. In addition to its
homeostatic and stress induced roles in protein folding, grp94
can function in the intracellular trafficking of peptides from
the extracellular space to the MHC class I antigen processing
pathway of antigen presenting cells. Strategies seeking to dis-
rupt Hsp90 activation of key pro-survival pathways hold promi-
se as either direct or adjuvant therapies for cancers displaying
altered Hsp90 expression.
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Applications
EKS-895 Hsp90a ELISA kit H
SPA-830 Hsp90 Monoclonal Antibody (AC88) H, M, R, C WB, IP, ICC, IHC, F
SPA-835 Hsp90 Rat Monoclonal Antibody (16F1) H, M, R, C, D WB, IP, ICC, IHC
SPA-845 Hsp90 Rat Monoclonal Antibody (2D12) H, M, R, C WB, IP
SPA-846 Hsp90 Polyclonal Antibody H, M, R, C WB
SPS-771 Hsp90a Polyclonal Antibody H, M, R, C, X WB, IP
SPA-840 Hsp90a Rat Monoclonal Antibody (9D2) H, C WB, IHC, F
SPA-843 Hsp90b Monoclonal Antibody (K3701) H, M, R WB, F
SPA-842 Hsp90b Monoclonal Antibody (K3705) H, M, R, C WB, IHC
SRA-1400 FKBP-59 (Hsp56, p59) Monoclonal Antibody H, M, R WB, IP, ICC, IHC
SPA-670 p23 Polyclonal Antibody H, M, R WB
SPP-776 Hsp90a Recombinant Protein H
SPP-770 Hsp90 Native Protein H
SPP-670 p23 Recombinant Protein H
HPK-102 Geldanamycin
HPK-101 17-AAG
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
HSP90AA1 Heat Shock Protein 90kDa a (cytosolic), class A member
HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP90A; HSP90N; HSPCAL1; HSPCAL4
3320 Nucleotide binding, Protein folding, Protein dimerization, Signal transduction
Broadly Cytoplasm, Nucleus
HSP90AA2 Heat Shock Protein 90kDa a (cytosolic), class A member 2
HSP90ALPHA, HSPCA, HSPCAL3
3324 Nucleotide binding, Protein folding
HSP90AB1 Heat Shock Protein 90kDa a (cytosolic), class B member 1
HSPC2; HSPCB; D6S182; HSP90B; FLJ26984; HSP90-BETA
3326 Nucleotide binding, Protein folding
Broad Cytoplasm
HSP90B1 Heat Shock Protein 90kDa b (Grp94), member 1
GP96; GRP94 7184 Ion binding, Anti-apopto-sis, Nucleotide binding, Ion sequestration , Protein folding, Protein transport
Broad Endoplasmic reticulum
Ischemic neuro-nal cell death
13WB: western blot, IP: immunoprecipitation, ICC: immunocytochemistry, IHC: immunohistochemistry, F: flow cytometry
Hsp90 (continued)
Hsp90a Monoclonal Antibody (Cat. No. SPA-840) Human colon cancer tissue was immunohistochemically stained
using Hsp90a monoclonal antibody (clone 9D2) at a dilution of
1:50.
Hsp90b Monoclonal Antibody (Cat. No. SPA-842)Human breast cancer tissue was immunohistochemically
stained using Hsp90b monoclonal antibody (clone K3705) at a
dilution of 1:50.
Hsp90Crystal structure of an Hsp90-Sba1 closed chaperone complex.
Nature (2006) 440(7087):1013-1017.
14
Hsp90a Monoclonal Antibody (Cat. No. SPA-840) Human colon cancer Coca-2 cells were analyzed by flow cytometry using isotype control antibody (left) or Hsp90a monoclonal
antibody (clone 9D2; right) at a final concentration of 10µg/mL.
Hsp110 belongs to a family of large stress proteins referred
to as the Hsp110/SSE (yeast stress seventy) family. Mammalian
Hsp110 shares approximately 30% amino acid identity with its
distant relative Hsp70, primarily in the conserved ATP-binding
domain. Hsp110 is one of the three or four most abundant
Hsps in mammalian tissue, with the highest constitutive ex-
pression in the brain. Functionally, Hsp110 appears to complex
with other chaperones (predominantly Hsp70 and Hsp25) to
maintain and repair protein folding. Hsp110 is more efficient
than Hsp70 in conferring heat resistance, and has been shown
to possess RNA-binding properties via the N-terminal ATP-
binding domain. Due to the inherent efficiency of Hsp110 in
binding peptide, the molecule has been utilized extensively as
an immunoadjuvant to deliver known tumor antigens to an-
tigen presenting cells, generating antigen-specific innate and
adaptive anti-tumor responses.
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
HSPH1 Heat Shock 105kDa/110kDa Protein 1
HSP105, HSP105A, HSP105B
10808 Nucleotide binding, Protein binding
Protein folding Broad Cytoplasm
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Applications
SPA-1101 Hsp110 Polyclonal Antibody H, M, R, B, Y WB, IP
SPA-1103 Hsp110 Polyclonal Antibody H, M, R, B, X WB
Hsp110
15datasheet: www.biomol.de www.antibodyworld.com
Chaperones & Others
The homeostatic process of protein folding and the protective functions of the protein folding machinery in stress-induced conditions (i.e. heat, starvation, oxidation) are dependent on heat shock proteins, as well as a diverse group of co-chape-rones and transcriptional regulators. These molecules inclu-de the Hsp70 co-chaperones HIP and HOP, the ER resident chaperones Calnexin and Calreticulin, and Protein Disulfide-
Isomerase (PDI). ER-resident chaperones are folded in the ER, and retained via their KDEL peptide motif which is bound by the KDEL receptor (Erd2p). Together with the Hsps, these molecules participate in proper glycoprotein folding, prevent premature oligomerization of nascent proteins, regulate Hsp co-chaperone substrate specificity, and promote the rearrange-ment of disulphide bonds in the secretory pathway.
Assay Designs (Stressgen) ProductsCat. No. Product Description Species Application
SPA-860 Calnexin Polyclonal Antibody H, M, R WB
SPA-865 Calnexin Polyclonal Antibody H, M, R, C, X WB, IP, ICC
SPA-600 Calreticulin Polyclonal Antibody H, M, R WB, IP, ICC, IHC
SPA-601 Calreticulin Monoclonal Antibody H WB, IP, ICC, IHC, F
VAP-SV003 CSP Polyclonal Antibody M, R, B, C, X WB, IP, IHC
SPA-585 ERp57 (Grp58) Polyclonal Antibody H, M, R, B WB
SPA-725 ERp57 (Grp58) Monoclonal Antibody H WB, IP, IHC
SPS-720 ERp72 Polyclonal Antibody H, M, R, B WB
SRA-1400 FKBP59 (Hsp56, p59) Monoclonal Antibody H, B WB, IP, ICC, IHC
SPA-240 GrpE Polyclonal Antibody E. coli WB, IP
SPA-766 Hip Polyclonal Antibody H, M, R, B WB
SRA-1500 HOP (p60) Monoclonal Antibody H, M, R, B, C, X W,B IP
SPA-950 HSF-1 Rat Monoclonal Antibody H, M, R, B WB, IP, ICC
SPA-901 HSF-1 Polyclonal Antibody H, M, R, B, C, D, X WB, IP, ICC
SPA-960 HSF-2 Rat Monoclonal Antibody H, M, R, B WB, IP
SPA-470 Hsp47 (Colligin) Monoclonal Antibody H, M, R, B WB, IHC
SPA-1040 Hsp104 Polyclonal Antibody Y WB, IP
SPA-827 KDEL Antibody (Grp78, Grp94) Antibody H, M, R, B, C, D, X WB, IP, ICC, IHC, F
VAA-PT048 KDEL Receptor Monoclonal Antibody H, M, R, B, C, D, X WB, IP, ICC
VAM-PT046 Membrin Monoclonal Antibody H, R, C WB, IP, ICC
SPA-670 p23 Polyclonal Antibody H, M, R WB
SPA-890 PDI Polyclonal Antibody H, M, R, B, X WB, IP, ICC
SPA-891 PDI Monoclonal Antibody H, M, R, B, C, X WB, ICC, IHC
VAM-SV021 Sec6 Monoclonal Antibody H, M, R, B, C WB, IP, ICC
CTA-123 TCP-1a Rat Monoclonal Antibody M, R, B WB, IP, ICC
CTA-191 TCP-1a Rat Monoclonal Antibody H, M, R, B, D, Y WB, IP, F
CTA-202 TCP-1b Rat Monoclonal Antibody H, M, R, B, C WB
VAP-PT068 UGGT Polyclonal Antibody M, R WB
SPP-767 Hip Recombinant Protein R
SRP-1510 HOP (p60) Recombinant Protein H
SPP-900 HSF-1 Recombinant Protein H
NSP-535 Hsp47 (Colligin) Recombinant Protein H
SPP-650 Active GrpE Recombinant Protein E. coli
SPP-670 p23 Recombinant Protein H
LYC-HL101 HeLa Cell Lysate (Heat Shocked)
16 H: human, M: mouse, R: rat, B: bovine, C: chicken, D: drosophila, Y: yeast
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
AHSA1 AHA1, activator of Heat Shock 90kDa Protein ATPase homolog 1 (yeast)
AHA1, C14orf3, p38
10598 ATPase activity, Protein folding, Chaperone activity, Protein binding
Broad Cytoplasm, Endoplasmic Reticulum
CABC1 chaperone, ABC1 activity of bc1 complex homolog (S. pombe)
ADCK3, COQ8 56997 Kinase activity, Protein folding, Nucleo-tide binding
Mitochondrion
CALR Calreticulin RO, SSA, cC1qR 811 DNA binding, Calcium homeostasis, Ion binding, Actin organization, Sugar binding, Protein export, Protein binding, Protein folding, Regulation of apoptosis, meiosis and transcription
Broad CytoplasmEndoplasmic reticulumExtracellular environment
CANX Calnexin CNX, IP90, P90 821 Ion binding, Angiogenesis, Sugar binding, Protein folding, Protein secretion
Broad CytoplasmEndoplasmic reticulumMembrane
CDC37 cell division cycle 37 homo-log (S. cerevisiae)
P50CDC37 11140 Protein binding, Protein folding, CDK activity
Cytoplasm
ClpP ClpP caseinolytic peptidase, ATP-dependent, proteolytic subunit homolog (E. coli)
8192 Endopeptidase activity, Proteolysis, Peptidase activity
Broad Mitochondrion
ClpX ClpX caseinolytic peptidase X homolog (E. coli)
10845 Ion binding, Protein folding, Nucleo-tide binding, Protein transport, Protein binding
Broad Mitochondrion
EXOC3 exocyst complex compo-nent 3 [Homo sapiens]
SEC6, SEC6L1, Sec6p
11336 Exocytosis, Protein transport Plasma mem-brane
FKBP1A FK506 binding protein 1A, 12kDa
FKBP1; PKC12; PKCI2; FKBP12; PPIASE; FKBP-12; FKBP12C
2280 Isomerase activity, Protein folding, Protein binding
Broad Cytoplasm, Sarcoplasmic Recticulum
FKBP1B FK506 binding protein 1B, 12.6 kDa
FKBP12.6, FKBP1L, FKBP9, OTK4, PKBP1L, PPIase
2281 Isomerase activity, Muscle contraction, Protein folding
Broadly Cytoplasm Hypertension
FKBP5 FK506 binding protein 5 FKBP51, FKBP54, P54, PPIase, Ptg-10
2289 FK506 binding, Protein folding, Isomerase activity, Protein binding
Broad Nucleus Depression
GOSR2 Golgi SNAP receptor com-plex member 2
Bos1, GS27, Membrin
9570 Receptor activity, Vesicle mediated trans-port, Transporter activity, Protein transport
Golgi apparatus, Endoplasmic reticulum, Mem-brane
HSF1 Heat Shock transcription factor 1
HSTF1 3297 DNA binding, Protein folding, Protein binding, Transcription, Transcriptional Activity
Broadly Cytoplasm, Nucleus
HSF2 Heat Shock transcription factor 2
3298 DNA binding, Protein folding, Protein binding, Transcription, Transcriptional Activity
Broadly Cytoplasm, Nucleus
HSF4 Heat Shock transcription factor 4
CTM 3299 DNA binding, Cell development, Transcriptional Activity, Cell proliferation, Protein folding, Transcription
Broad Nucleus
HSPA4L Heat Shock 70kDa Protein 4-like
APG-1, Osp94 22824 Nucleotide binding, Protein folding Broad Cytoplasm, Nucleus
HSPBP1 Hsp70-interacting Protein 23640 Broad
KDELR1 KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1 [Homo sapiens]
ERD2, ERD2.1, HDEL, PM23
10945 ER retention, Protein retention, Protein transport
Endoplasmic reticulumGolgi apparatus
KDELR2 KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 2 [Homo s apiens]
ELP-1; ERD2.2 11014 ER retention, Protein retention, Protein transport
Endoplasmic reticulumGolgi apparatus
KDELR3 KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 3 [Homo sapiens]
ERD2L3 11015 ER retention, Protein retention, Protein transport
Endoplasmic reticulumMembrane
PDIA2 Protein disulfide isomerase family A, member 2
PDA2, PDI, PDIP, PDIR
64714 Isomerase activity, Apoptosis, Protein binding, Redox homeostasis, Protein folding, Protein retention
Endoplasmic reticulum
17WB: western blot, IP: immunoprecipitation, ICC: immunocytochemistry, IHC: immunohistochemistry, F: flow cytometry
Chaperones & Others (continued)
Grp94 Monoclonal Antibody (Cat. No. SPA-850)Human colon cancer CoCa-2 cells were analyzed by flow cytometry using isotype control antibody (left) or
Grp94 monoclonal antibody (clone 9G10; right) at a final concentration of 10µg/mL.
Official Symbol Name Synonyms
Entrez Gene ID Biological Function
Tissue Distribution
Cellular Distribution
Human Diseases
PDIA3 Protein disulfide isomer-ase family A, member 3
ERp57, ERp60, ERp61, GRP57, GRP58, P58, PI-PLC
2923 Cysteine endopeptidase activity, Re-dox homeostasis, Phospholipase C ac-tivity, Regulation of apoptosis, Protein binding, Protein import into nucleus, Disulfide isomerase activity, Protein retention in ER, Signal transuction
Broad Endoplasmic reticulum
PDIA3P Protein disulfide isomer-ase family A, member 3 pseudogene
Erp60, GRP58P 171423
PDIA4 Protein disulfide isomer-ase family A, member 4
Erp70, Erp72 12304 Ion binding, Redox homeostasis, Isomerase activity, Protein secretion, Protein disulfide isomerase activity
Endoplasmic reticulum
PDIA5 Protein disulfide isomer-ase family A, member 5
FLJ30401, PDIR 10954 Isomerase activity, Electron transport, Oxidoreductase activity, Redox ho-meostasis, Protein folding
Endoplasmic reticulum
PDIA6 Protein disulfide isomer-ase family A, member 6
ERP5, P5, TXNDC7
10130 Isomerase activity, Redox homeostasis, Protein folding
Endoplasmic reticulum
PTGES3 Prostaglandin E synthase 3 (cytosolic)
P23, TEBP 10728 Isomerase activity, Fatty acid bio-synthesis, Prostaglandin E sytnhase, Prostanoid biosynthesis, Telomerase activity, Signal transduction, Telomere maintenance
Cytoplasm, Nucleus
STIP1 Stress-induced-phospho-protein 1 (Hsp70/Hsp90-organizing protein)
HOP; P60; STI1L 10963 Binding, Response to stress, Protein folding
Golgi, Nucleus
TCP1 t-complex 1 CCT-a, CCT1, CCTa, TCP-1-a
6950 Nucleotide binding, Protein folding Cytoplasm
TOR1A torsin family 1, member A (torsin A)
DQ2, DYT1, torsin A
1861 Endopeptidase activity, Protein folding, Nucleotide binding
Broad Cytoplasmic,, Endoplasmic Reticulum
Dystonia
TOR1B torsin family 1, member B (torsin B)
DQ1 27348 Nucleotide binding, Protein folding Endoplasmic Reticulum
TRAP1 TNF receptor-associated Protein 1
HSP75, HSP90L 10131 Nucleotide binding, Protein folding Broad Mitochondrion
UGCGL1 UDP-glucose ceramide glucosyltransferase-like 1
HUGT1 56886 Glucosyltransferase activity, Protein folding, Amino acid glysoylation
Broad Endoplasmic reticulum
UGCGL2 UDP-glucose ceramide glucosyltransferase-like 2
HUGT2 55757 Glucosyltransferase activity, Protein folding, Amino acid glysoylation
Broad Endoplasmic reticulum
18
TCP-1a Monoclonal Antibody (Cat. No. CTA-191)Human colon cancer Coca-2 cells were analyzed by flow cytometry using isotype control antibody
(left) or TCP-1a monoclonal antibody (clone 91a; right) at a final concentration of 10µg/mL.
Grp75 Monoclonal Antibody (Cat. No. SPS-825)Human breast cancer tissue was immunohistochemically
stained using Grp75 monoclonal antibody (clone 30A5) at a
dilution of 1:50.
19datasheet: www.biomol.de www.antibodyworld.com
Heat shock proteins (HSP), also known as molecular chape-
rones, are critical regulators of cellular homeostasis. Initially
identified some forty years ago as heat responsive genes, HSPs
have been reported to play important roles in the folding of
nascent or new proteins, guiding the renaturation of mis-
folded or partly denatured proteins, as well as facilitating
cellular turnover of client proteins8,12,14. In this regard, HSP90
and its associated co-chaperone complex is known to recruit E3
ubiquitin ligases under certain conditions, favoring the ubiqu-
itinylation and degradation of the client proteins. However, in
the presence of ATP, HSP90 complexes can favor the stabiliza-
tion of these client proteins23.
HSPs are categorized into six different families according to
their respective molecular weights. They are the HSP100 fami-
ly, the HSP90 family, the HSP70 family, the HSP60 family, the
HSP40 family, and the small heat shock family (sHSPs) including
HSP27.
Small Heat Shock FamilyThe small heat shock family (sHSP) of molecular chaperones is
a ubiquitously expressed group of proteins that is highly con-
served among species. To date, ten sHSP isoforms have been
identified and designated HSPB1 through HSPB10, respectively,
with the most common being HSPB1 or HSP27, and HSPB5 or
aB-crystallin14. Both HSP27 and aB-crystallin are constitutively
expressed in a variety of tissues; their expression, however,
is also up-regulated under conditions of stress as well as in a
variety of disease settings14.
Members of the sHSP family are categorized on the basis that
they possess a conserved C-terminal region known as the a-cry-
stallin domain and a variable N-terminal region. The a-crystal-
lin domain consists of two anti-parallel b-sheets14. It is worth
noting that while proteins like HSP32/HO-1 have also been
categorized as sHSPs, they lack the critical C-terminal a-crystal-
lin domain defining this family of heat shock proteins.
The small heat shock family members vary in their respective
molecular weights; they range in size from 15 kDa to 30 kDa.
These proteins are known to exist as either homo- or hetero-
complexes ranging in size from single units to large multimeric
complexes up to approximately 700 kDa3.
It is well documented that sHSP family members undergo
post-translational modifications with the most common being
the phosphorylation of serine residues. For instance, both the
human form of aB-crystallin and HSP27 are phosphorylated on
three serine residues. In the case of aB-crystallin, this protein is
phosphorylated on Ser-19, Ser-45, and Ser-5913; whereas HSP27
is phosphorylated on Ser-15, Ser-78, and Ser-82, respective-
ly16,22.
While little homology exists in the sequences flanking these
phosphorylation sites, there is definite overlap in regard to the
kinases that phosphorylate these sites. In particular, the mito-
gen activated protein kinase activated protein kinase, MAP-
KAPK-2 is one of the key protein kinases able to phosphorylate
many of these sites with the exception of Ser-19 on aB-crystal-
lin, both in vitro and in vivo. At present, the kinase responsible
for phosphorylating Ser-19 of on aB-crystallin has yet to be
identified. Other kinases implicated in the phosphorylation of
these serine sites are Erk-1 and Erk-2, which phosphorylate aB-
crystallin15, and MAPKAPK-3, PKAca, p70S6K, PKD1, and PKCd,
which phosphorylate HSP276,9,16,21,22.
Upstream Signals Leading to the Phosphorylation of HSP27HSP27 has been reported to be phosphorylated in response
to a variety of extracellular-derived signals including TNFa,
thrombin, bFGF stimulation, as well as under conditions of
heat shock and oxidative stress7,16. It is postulated that these
pathways converge on and elicit their effects through p38
MAPK and MAPKAPK-2. p38 MAPK has been reported to phos-
phorylate MAPKAPK-2 in vitro on several residues including
Thr-25, Thr-222, and Thr-334 leading to its activation5. Upon
activation, MAPKAPK-2 is believed to phosphorylate HSP27 in
Hsp27 Review
HSP27: A regulator of cellular invasion. HSP27 localizes to focal
adhesions, influences membrane dynamics and enhances the invasive
phenotype of malignant cells.
20
vivo. MAPKAPK-2, as well as MAPKAPK-3, has been reported
to phosphorylate HSP27 in vitro on all three HSP27 phosphory-
lation sites, Ser-15, Ser-78, and Ser-8216,22. Studies utilizing the
p38 inhibitor, SB203580, have also offered conclusive evidence
that the p38 pathway is intimately involved in the post-trans-
lational regulation of HSP27. Treatment with SB203580, is able
to attenuate the phosphorylation of HSP27 in response to
various agonists18.
More recently, both PKD1 and AKT1 have been ascribed as
HSP27 phosphorylating kinases. PKD1 was shown to phospho-
rylate HSP27 in vitro, however, only on Ser-15 and Ser-829.
AKT1, on the other hand, was shown to interact with p38 and
phosphorylate HSP27 on Ser-8221.
HSP27: FunctionAs a high molecular weight complex, HSP27 plays a critical role
in the renaturation of misfolded or partly denatured proteins
by specifically blocking their aggregation10. As with other
phospho-proteins, this function is tightly linked with the phos-
phorylation status of HSP27. Phosphorylation of Ser-82 has
been shown to result in HSP27 complex dissociation and the
subsequent loss of its chaperoning activity. In addition to its
chaperoning function, HSP27 has been shown to interact with
different cytoskeletal elements affecting actin polymerization4
as well as inhibiting apoptosis7,19,20.
Apoptosis, or programmed cell death, is a finely coordina-
ted process involving the activation of a discrete network of
enzymes, referred to as cellular caspases, that aid in preserving
the fidelity of the human genome as well as turning over
damaged or worn-out cells. While there is variation in terms of
the mechanism by which apoptosis can be elicited (e.g., death
receptor apoptosis vs. mitochondrial mediated apoptosis),
these pathways converge on the key executioners of apoptosis,
caspases-3, –6 and –7, to carry out the process. To counteract
these pro-apoptotic mechanisms, the cell has devised a number
of ways to inhibit this process. Two of the best-defined mecha-
nisms involve the overexpression of the B-cell lymphoma pro-
tein, Bcl-2 and the activation of the anti-apoptotic kinase, AKT.
More recently, HSP27 has also been ascribed as an anti-apopto-
tic protein. In particular, HSP27 has been reported to inhibit
apoptosis (1) through its interactions with the death associated
protein DAXX7, (2) by facilitating the activation of AKT21, and
(3) by blocking the formation of the apoptosome19,20. Taken
together, the overexpression of HSP27 in the context of a
disease such as cancer, would facilitate adaptation to stressful
conditions by aiding in the suppression of apoptosis, ultimately
leading to a more aggressive phenotype. As such, it is not sur-
prising that the overexpression of HSP27 correlates with poor
patient prognosis in a variety of lesions.
HSP27: Clinical RamificationsThere is a wealth of evidence supporting the notion that heat
shock proteins may contribute to the pathogenesis of human
diseases like cancer, cardiovascular disease, and neurological
disorders. Moreover, elevated expression of certain HSPs, like
HSP27, has been reported to correlate with poor patient out-
come in breast, ovarian, and prostate cancer8. This might, in
part, be due to the effects HSP27 has on the cytoskeleton.
Recently, HSP27 has been reported to behave as an actin-cap-
ping protein and influence actin dynamics; the latter of which
was shown to be dependent upon the phosphorylation status
of HSP274,17. In this regard, unphosphorylated monomeric
HSP27 was shown to inhibit the polymerization of actin in
vitro, whereas multimeric HSP27 complexes appeared to have
no inherent effect on actin dynamics regardless of phosphory-
lation status. HSP27 has also been demonstrated to localize to
focal adhesions, influence membrane dynamics, as well as in-
fluence invasive phenotype of cells2,11,24. More recently, HSP27
has been shown to play a role in the regulation of matrix
metalloproteinase (MMP)-2 activity in prostate cancer cells24.
Taken together, it would appear that disrupting the interac-
tions between HSP27 and its binding partners, or reducing its
expression in cancer might be a therapeutically valid approach
when combined with conventional methodologies.
HSP27: Phosphorylation linked to function. HSP27 is phosphorylated
on key serine residues by MAPKAPK2 as well as MAPKAPK3 amongst
others. Phosphorylation is associated with the dimerization of HSP27 and
its function.
References on page 26
21
Initially identified by Ritossa some forty years ago, heat shock
proteins (HSP) were first identified as genes up-regulated in
response to heat shock stimulation in Drosophila20. They are
now recognized as proteins that play critical roles in cellular
homeostasis and the adaptation to stressful conditions such as
heat shock, oxidative stress, genotoxic shock, viral infection,
and hypoxic conditions26. In part, the cytoprotective effects of
HSPs are achieved through their role in the re-folding of partly
denatured or misfolded proteins. HSPs are also known to be
involved in: (1) the folding of newly formed proteins, (2) the
trafficking of cellular proteins, as well as (3) the turn over of
cellular proteins through the proteasomal pathway; as such,
HSPs have been classified as “molecular chaperones”.
HSPs are ubiquitously expressed and highly conserved among
species, ranging from the simplest prokaryotes to complex eu-
karyotes such as humans. They are classified according to their
respective molecular weights and are divided into six families:
the small HSPs (sHSPs), the HSP40 family, the HSP60 family, the
HSP70 family, the HSP90 family, and the HSP100 family.
The HSP70 FamilyThe HSP70 family represents one of the most widely examined
heat shock families and consists of up to ten highly homolo-
gous members. Refer to Table 1 for a representative list of the
HSP70 family members.
As with other heat shock families, members of the HSP70 fami-
ly differ in their spatial and subcellular distribution, as well as
their expression levels under normal, unstressed conditions21,24.
It is well established that the expression of some members of
the HSP70 family can be induced under conditions of stress;
as these proteins do not contain introns, they are able to be
quickly up-regulated.
While the expression of many HSP70 family members can be
up-regulated in response to various stressors, the major stress
inducible HSP70 members are the highly homologous genes
HSP1A1 and HSPA1B, also referred to as HSP70-1 and HSP70-2,
respectively. These proteins are expressed at relatively low or
undetectable levels in most normal, unstressed cells; however,
upon insult, their expression dramatically increases. It is worth
noting, that HSPA6 and HSPA7, the two other highly related
HSP70 inducible members known as HSP70B’ and HSP70B are
up-regulated only under conditions of extreme stress21,24. At
present, further research is required to elucidate the physiolo-
gical importance of these two HSP70 family members.
The constitutively expressed member of HSP70 family is HSPA8,
also referred to as HSC70. HSC70 is ubiquitously expressed in
all cell types and is believed to be responsible for maintaining
normal cellular function. Two other members of the HSP70 fa-
mily under active investigation are the endoplasmic reticulum-
(ER) and mitochondrial-associated members, referred to as the
glucose regulated proteins, GRP78 and GRP75. GRP78 plays
a critical role in the ER-associated stress response, whereas
GRP75 (also known as mortalin) is involved in the maintenance
of mitochondrial function.
HSP70: Structure and FunctionAll HSP70 family members contain a highly conserved N-termi-
nal ATPase domain of approximately 44 kDa which possesses
weak ATPase activity under normal conditions. These proteins
also contain an approximately 25 kDa C-terminal region which
consists of a conserved hydrophobic peptide binding domain
(PBD) of approximately 15 kDa, and a more variable a-helical
domain of approximately 10 kDa5. The a-helical domain is
classified as a “cap” believed to open and close in response to
changes in the nucleotide binding status of HSP7015.
The activity and function of HSP70 are thought to result from
the binding of ATP to the N-terminus. In its ATP-bound state,
the C-terminus of HSP70 is said to undergo a conformational
change, resulting in the opening of the a-helical cap; this
opening allows substrates to interact with the hydrophobic
pocket of the PBD. In its ADP-bound state, it is believed that
the a-helical cap is closed, excluding substrates from the PBD.
Thus, in the presence of ATP, HSP70 is said to favor the folding
of its client protein, as it has a lower affinity and faster proces-
sing rate than the ADP-bound form5,15. However, unlike other
enzyme classes, members of the HSP70 family bind to a wide
variety of client proteins through short hydrophobic segments
found in unfolded, misfolded, or denatured proteins.
On its own, members of the HSP70 family are known to
possess little or no intrinsic ATPase activity. As with other heat
shock proteins, ATPase activity and function are thought to
be influenced through interactions with specific co-chaperone
molecules.
HSP70 co-chaperones include: (1) HSP40, which is believed
to assist in loading targets on the HSP70 machinery3, (2) the
HSC70 interacting protein, Hip, which binds to the ATPase do-
main stimulating its activity3, (3) the HSC70/HSP90 organizing
protein, Hop, which serves as a link between HSP70 and HSP90
allowing for substrate exchange between the two chaperones,
and also facilitates ATP/ADP cycling3, (4) the HSC70 unbin-
ding protein, Hup, which facilitates the release of unfolded
proteins3 , (5) the HSC70 accessory protein, Hap3, and the Bcl-2
associated athanogene proteins, BAG-1, BAG-2, and BAG-3,
which interact with the ATPase domain and block the binding
of unfolded proteins4,11,23,27, and (6) the carboxyl-terminus of
HSP70 interacting protein, CHIP, which is believed to be a bona
Hsp70 Review
22
fide E3 ubiquitin ligase assisting in the ubiquitinylation of
cellular proteins1,10,16.
Overall, members of the HSP70 family are known to play
critical roles in the folding of newly synthesized proteins; the
re-folding of misfolded or denatured proteins; the trafficking
of proteins across cellular membranes; the disassembly of
clathrin-coated vesicles; the inhibition of protein aggregation;
and the targeting and degradation of proteins via the protea-
somal pathway3. More recently, HSP70 has also been demons-
trated to suppress apoptosis in response to various stimuli12.
HSP70: Effects on ApoptosisApoptosis is a highly coordinated process that functions either
through the activation of a discrete network of cysteine pro-
teases known as cellular caspases, or through mechanisms not
depending on caspase activation, known as caspase-indepen-
dent cell death.
The activation of cellular caspases can be achieved through va-
rious mechanisms including death signals provided at the level
of the cell membrane, the mitochondria, and the endoplasmic
reticulum. While these pathways rely on different initiators
of apoptosis, they all converge on, and elicit their effects
through, the executioner caspases — mainly caspase-3, -6 and
-7. Along with the activation of endonucleases, the activation
of these caspases results in the dismantling of the cell and its
intracellular contents, leading to the eventual formation of
apoptotic bodies.
It is well established that the commitment to undergo apopto-
sis can be attenuated or blocked through various mechanisms,
including the activation of key signal transduction molecules
such as Akt, and the overexpression of certain cellular prote-
ins such as Bcl-2. More recently, overexpression of heat shock
proteins — mainly members of the HSP70 family — has also
been demonstrated to inhibit apoptosis. Elevated expression
of HSP70 has been reported to: (1) inhibit the formation of the
apoptosome2, (2) inhibit the translocation of the Bcl-2 protein,
Bax, to the mitochondrial membrane, ultimately blocking the
release of cytochrome c from the mitochondria22, (3) inhibit
the activation of cellular caspases19, (4) block the activation
of the apoptosis signal regulating kinase, ASK118, (5) inhibit
the activation of the stress kinase p388, and (6) inhibit JNK
activation17.
HSP70: Clinical Ramifications in CancerThere is a wealth of literature supporting the notion that heat
shock proteins are elevated in a variety of human malignancies
and that these increases in expression may not only contribute
to the pathogenesis of the disease25, but may be of diagnostic,
prognostic and therapeutic importance6. In this regard, HSP70
has been reported to correlate with poor differentiation in
certain malignancies, increased lymph node metastases, che-
mo-resistance, and poor clinical outcome6,14. Further studies
evaluating the importance of HSP70 family members in the
initiation and progression of cancer will undoubtedly be of
great clinical importance.
HSP70: A cell survival protein. HSP70
suppresses apoptosis by inhibiting the
formation of the apoptosome and by
blocking the activation of stress induced
kinases including: ASK1, p38, and JNK,
respectively.
References on page 26
23datasheet: www.biomol.de www.antibodyworld.com
The heat shock, or stress family of proteins is a highly conser-
ved, ubiquitously expressed class of proteins that have been
demonstrated to be intimately involved in the regulation of
cellular homeostasis in response to a myriad of environmental
and physiological stressors27.
The heat shock proteins (HSP) are classified into six different
groups according to their respective molecular weights; they
are the small heat shock proteins including HSP27, the HSP40
family, the HSP60 family, the HSP70 family, the HSP90 family,
and the HSP100 family, respectively.
HSPs, commonly referred to as molecular chaperones, were
initially identified and described over thirty years ago as heat
shock responsive genes. HSPs are now know to play critical
roles in the stabilization of partly denatured or misfolded pro-
teins, facilitate proper folding of nascent or new polypeptides
as well as regulate the spatial distribution of cellular proteins.
More recently, these molecular chaperones, mainly HSP90,
have received significant attention for the putative roles they
play in the pathogenesis and progression of human diseases
like cancer21,35.
HSP90: Structure and FunctionThe HSP90 family, which consists of both inducible and consti-
tutive isoforms, is encoded at two distinct loci. Cellular ho-
mologues of the HSP90 family include: HSP90a (the inducible
isoform), HSP90b (the constitutive isoform) Grp94 and Trap1,
as well as the recently identified variant HSP90N. Whereas,
HSP90a and HSP90b are predominantly cytosolic proteins and
represent 1-2% of the normal cellular protein content, Grp94
and Trap1 are localized within the endoplasmic reticulum (ER)
and mitochondria, respectively, and are expressed at much
lower levels than their cytoplasmic counterparts28. HSP90N, on
the other hand, preferentially localizes to the cellular membra-
ne through its unique N-terminal hydrophobic region10.
All members of the HSP90 family possess three specific do-
mains: an N-terminal nucleotide binding pocket to which most
clinical compounds are being developed6,22, a central domain
important for ATPase activity11,19, and a C-terminal domain
believed to act as a second nucleotide binding site9. HSP90
can either exist as a homodimer, a heterodimer, or as a multi-
protein complex with other co-chaperones including HSP40,
HSP70, Hop, and p2328. As with other heat shock families, di-
merization is believed to be an ATP-dependent process. Unlike
other member; however, the N-terminal nucleotide binding
site of HSP90 is highly unique and bears a strong resemblance
to members of the GKHL superfamily including bacterial gyra-
se, MutL and histidine kinases8.
The mechanism(s) involved in regulating HSP90 activity and
function, is at present unclear. However thought to involve:
(1) post-translational modification including acetylation and
phosphorylation1,17,20, (2) the N-terminal nucleotide binding
status28, and (3) interactions with accessory co-chaperones28.
Early studies evaluating the phosphorylation status of HSP90
revealed that phosphorylation of this target is essential for its
activity. In this regard, HSP90 has been reported to be tyrosine
phosphorylated in vivo when complexed with other proteins1.
These specific phosphorylation sites have yet to be elucidated,
however. More recently, the acetylation status of HSP90 has
also been reported to influence the activity of HSP90. In par-
ticular, these studies revealed that hyperacetylation of HSP90
led to decrease in its association with the essential co-chapero-
ne, p23, and a concomitant loss of chaperoning activity20. The
specific acetylation sites have been yet to be reported.
The N-terminal nucleotide binding status has also been de-
monstrated to influence the function of HSP90. In the presence
of ATP and the appropriate upstream signals, HSP90 cyclizes
with its co-chaperone molecules, stabilizing the expression
of its client proteins. However, when bound by inhibitors like
Hsp90 Review
left: HSP90: A regulator of cell survival.
Inhibition of HSP90 activity by drugs like
geldanmycin destabilize client proteins which
ultimately leads to the onset of apoptosis.
right: HSP90: A “drugable” target. Inhibi-
tion of HSP90 by geldanmycin (GA) favors
the ubiquitinylation and degradation of client
proteins.
24
Geldanamycin (GA), HSP90 function is impaired which results
in the recruitment of E3 ubiquitin ligases favoring the ubi-
quitinylation and degradation of client proteins by the 26S
proteasomal complex28. The stabilization versus degradation
of proteins, in the presence of physiological stressors, may tip
the balance in favor of stabilizing mutant proteins ultimately
promoting an anti-apoptotic or pro-survival state.
As with other heat shock proteins, HSP90 requires a numb-
er of co-chaperone molecules for its full function including
HSP70, HSP40, Hip/Hop, p23, immunophilins, and CDC37/p5028.
More recently, Aha1 (Activator of HSP90 ATPase homologue
1), which associates with the central domain of HSP90, was
identified as a key molecular co-chaperone required for ATPase
function18.
HSP90: Client ProteinsIn comparison to other members of the heat shock family,
HSP90 client proteins are unique and tend to encompass key
signal transduction molecules involved in the regulation of
cellular growth, survival, and differentiation. In this regard,
one of the first client proteins to be described was the trans-
forming tyrosine kinase isolated from the Rous sarcoma virus,
v-Src30,33. Since this original discovery, the number of client
proteins influenced by HSP90 has significantly increased, many
of which are linked with the pathogenesis of human cancer.
Client proteins include serine/threonine and tyrosine kinases,
transcription factors, and steroid receptors as well as certain
tumor suppressor proteins. A concise list of clients influenced
by HSP90 include: Akt/PKB, ASK1, Aurora B, Bcr-Abl, CDK1,
CDK4, CHK1, CKII, ErbB2/Her-2, EGFR, ER, Hif-1a, c-Met, mu-
tant p53, PLK, and Raf28.
Two key signaling molecules influenced by HSP90, which are
central to normal physiology, are the protein kinase Akt, and
the tumor suppressor protein p53. In the case of Akt, HSP90
has been demonstrated to bind with the phosphorylated form
and protect it from being inactivated by its dephosphorylating
phosphatase, protein phosphatase (PP)-2A25. When active, Akt
is known to provide anti-apoptotic signals, through various
mechanisms, ultimately preventing the cells from undergoing
apoptosis. In this regard, Akt in association with HSP90, has
been demonstrated to phosphorylate and inhibit the apoptotic
kinase ASK1, thus blocking apoptosis36.
In the case of p53, HSP90 has been reported to bind with and
stabilize the expression of the mutated form of this prote-
in29. Stabilization of the mutated form provides a mechanism
of knocking out the function of the normal wild-type p53
molecules through a dominant-negative effect. Functional p53
exists as a tetramer; as such, one mutated copy of p53 within
this complex is capable of impairing normal p53 function. As
p53 has been marked as the master regulator of the human
genome, knocking out this function of this essential prote-
in through stabilization of the mutated form allows for the
propagation of additional favorable oncogenic mutations,
including those that facilitate progression of the disease e.g.,
invasion and metastasis.
HSP90: Clinical Ramifications in CancerSeveral lines of evidence support the notion that the expressi-
on levels of heat shock proteins are dramatically increased in
a variety of human malignancies, both in solid and hematolo-
gical types, and might contribute to the advancement of the
disease3,5,7,12,15,16,21,23,24,26,34,35. As an example, elevated levels
of HSP27 have been reported to correlate with poor patient
outcome in prostate, breast, and ovarian cancer4. Moreover,
compelling evidence suggests that HSP90, in the context of
cancer, exists in a “hyperactive state” in the diseased tissue
when compared with the normal surrounding material14. In
its highly active state, the HSP90 complex would theoretically
influence key signaling nexuses that would contribute to the
pathogenesis of the disease; these include cell growth promo-
tion, evasion of apoptosis, and stimulation of angiogenesis. In
this regard, it has been postulated that changes in expression
and activity levels are critical in that they provide a mechanism
to counteract, or compensate, for the selective pressures these
abnormal cells experience as the disease progresses including
gene mutations, hypoxia, and growth pressures amongst
others. As such, heat shock proteins, mainly HSP90, appear
to provide a buffering mechanism facilitating the “natural
selection” of the strongest cell lineage ultimately allowing for
adaptation to the “harshest” of conditions.
Consequently, based upon the uniqueness of the N-terminal
nucleotide binding site, the differences in biological activity
between the cancer and normal tissue, and the notion that
HSP90 stabilizes key oncogenic client proteins, HSP90 has been
suggested to serve as an excellent target for therapeutic in-
tervention2,13,31. Not only is targeting HSP90 selecting against
those adaptable cell lineages, but in addition, key oncogenic
proteins would be destabilized and consequently degraded,
shifting the balance towards an anti-proliferative pro-apopto-
tic state.
Currently, there are on-going clinical trials evaluating the
efficacy of these N-terminal specific inhibitors and a number
of clinical candidates in the pipeline. Perhaps, the future will
entail a combinatorial modality involving the administration of
selective HSP90 inhibitors with conventional methodologies.
References on page 26
25
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26. Wegele H, Muller L, Buchner J. Hsp70 and Hsp90--a relay team for protein folding. Rev Physiol Biochem Pharmacol. 2004;151:1-44.
27. Zeiner M, Gebauer M, Gehring U. Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 1997 Sep 15;16(18):5483-5490.
Hsp90 References1. Adinolfi E, Kim M, Young MT, Di Virgilio F, Surprenant A. Tyrosine phosphorylation of HSP90 within the P2X7 receptor complex negatively regulates P2X7 receptors. J Biol Chem. 2003 Sep 26;278(39):37344-51.
2. Bagatell R, Whitesell L. Altered Hsp90 function in cancer: a unique therapeutic opportu-nity. Mol Cancer Ther. 2004 Aug;3(8):1021-30.
3. Chant ID, Rose PE, Morris AG. Analysis of heat-shock protein expression in myeloid leukaemia cells by flow cytometry. Br J Haematol. 1995 May;90(1):163-8.
4. Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones. 2005 Jun; 10(2): 86-103.
5. Ciocca DR, Clark GM, Tandon AK, Fuqua SA, Welch WJ, McGuire WL. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J Natl Cancer Inst. 1993 Apr 7;85(7):570-4.
6. Chadli A, Bouhouche I, Sullivan W, Stensgard B, McMahon N, Catelli MG, Toft DO. Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90. Proc Natl Acad Sci U S A. 2000 Nov 7; 97(23): 12524-12529.
7. Conroy SE, Sasieni PD, Fentiman I, Latchman DS. Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients. Eur J Cancer. 1998 May;34(6):942-3.
8. Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci. 2000 Jan;25(1):24-8.
9. Garnier C, Lafitte D, Tsvetkov PO, Barbier P, Leclerc-Devin J, Millot JM, Briand C, Maka-rov AA, Catelli MG, Peyrot V. Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. J Biol Chem. 2002 Apr 5;277(14):12208-14.
10. Grammatikakis N, Vultur A, Ramana CV, Siganou A, Schweinfest CW, Watson DK, Raptis L. The role of Hsp90N, a new member of the Hsp90 family, in signal transduction and neoplastic transformation. J Biol Chem. 2002 Mar 8;277(10):8312-20.
11. Huai Q, Wang H, Liu Y, Kim HY, Toft D, Ke H. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure. 2005 Apr;13(4):579-90.
12. Jameel A, Skilton RA, Campbell TA, Chander SK, Coombes RC, Luqmani YA. Clinical and biological significance of HSP89 a in human breast cancer. Int J Cancer. 1992 Feb 1;50(3):409-15.
13. Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med. 2004 Jun;10(6):283-90.
14. Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, Burrows FJ. A high-affi-nity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature. 2003 Sep 25;425(6956):407-10.
15. Kaur J, Ralhan R. Differential expression of 70-kDa heat shock-protein in human oral tumorigenesis. Int J Cancer. 1995 Dec 11;63(6):774-9.
16. Kimura E, Enns RE, Alcaraz JE, Arboleda J, Slamon DJ, Howell SB. Correlation of the survival of ovarian cancer patients with mRNA expression of the 60-kD heat-shock protein HSP-60. J Clin Oncol. 1993 May;11(5):891-8.
17. Lees-Miller SP, Anderson CW. Two human 90-kDa heat shock proteins are phosphory-lated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem 1989 Feb; 264(5): 2431-7
18. Meyer P, Prodromou C, Liao C, Hu B, Mark Roe S, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 2004 Feb 11;23(3):511-9.
19. Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell. 2003 Mar;11(3):647-58.
20. Murphy PJ, Morishima Y, Kovacs JJ, Yao TP, Pratt WB. Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chapero-ne. J Biol Chem. 2005 Oct 7;280(40):33792-9.
21. Nanbu K, Konishi I, Mandai M, Kuroda H, Hamid AA, Komatsu T, Mori T. Prognostic significance of heat shock proteins HSP70 and HSP90 in endometrial carcinomas. Cancer Detect Prev. 1998;22(6):549-55.
22. Prodromou C, Roe SM, O’Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 1997 Jul 11;90(1):65-75.
23. Ralhan R, Kaur J. Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix. Clin Cancer Res. 1995 Oct;1(10):1217-22.
24. Santarosa M, Favaro D, Quaia M, Galligioni E. Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients. Eur J Cancer. 1997 May;33(6):873-7.
25. Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A. 2000 Sep 26;97(20):10832-7.
26. Trieb K, Gerth R, Holzer G, Grohs JG, Berger P, Kotz R. Antibodies to heat shock prote-in 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy. Br J Cancer. 2000 Jan;82(1):85-7.
27. Wegele H, Muller L, Buchner J. Hsp70 and Hsp90--a relay team for protein folding. Rev Physiol Biochem Pharmacol. 2004;151:1-44.
28. Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer. 2005 Oct;5(10):761-72.
29. Whitesell L, Sutphin PD, Pulcini EJ, Martinez JD, Cook PH. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol. 1998 Mar;18(3):1517-24.
30. Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansa-mycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A. 1994 Aug 30; 91(18): 8324-8328.
31. Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med. 2004 Feb;10(2):47-51.
32. Xu W, Marcu M, Yuan X, Mimnaugh E, Patterson C, Neckers L. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12847-52.
33. Xu Y, Singer MA, Lindquist S. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc Natl Acad Sci U S A. 1999 Jan 5;96(1):109-14.
34. Yano M, Naito Z, Tanaka S, Asano G. Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res. 1996 Sep;87(9):908-15.
35. Yufu Y, Nishimura J, Nawata H. High constitutive expression of heat shock protein 90 a in human acute leukemia cells. Leuk Res. 1992 Jun-Jul;16(6-7):597-605.
36. Zhang R, Luo D, Miao R, Bai L, Ge Q, Sessa WC, Min W. Hsp90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis. Oncogene. 2005 Jun 2;24(24):3954-63.
27datasheet: www.biomol.de www.antibodyworld.com
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Heat Shock Proteins and Molecular Chaperones Price List
CTA-123DCTA-123FCTA-191DCTA-191FCTA-202CCTA-202EEKS-500EKS-600EKS-650EKS-700BEKS-725EKS-750EKS-800EKS-810EKS-895ESP-502DESP-502EESP-540DESP-540EESP-555DESP-555FESP-581DESP-581FESP-715DESP-715FESP-741DESP-741EHPK-101JHPK-102JLYC-HL101FNSP-510BNSP-510FNSP-535BNSP-535FNSP-540BNSP-540ENSP-550BNSP-550ENSP-555BNSP-555EOSA-110COSA-110EOSA-111BCOSA-111BEOSA-111COSA-111EOSA-111FICOSA-111FIEOSA-150EOSA-200COSA-200ESPA-110DSPA-110FSPA-210DSPA-210F
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175372175372175372753753753890897753753753864415599415599415
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Anti-TCP-1alpha (CCT), clone 23c (Rat IgG2c)Anti-TCP-1alpha (CCT), clone 23c (Rat IgG2c)Anti-TCP-1alpha (CCT), clone 91a (Rat IgG2a)Anti-TCP-1alpha (CCT), clone 91a (Rat IgG2a)Anti-TCP-1beta, clone PK/8/4/4i/2fAnti-TCP-1beta, clone PK/8/4/4i/2fHsp27 StressXPress ELISA KitHSP60 Antigen StressXPress ELISA KitAnti-Human Hsp60 (total) StressXPress ELISA KitHsp70 StressXPress ELISA kit (B-version)Hsp70B‘ StressXPress ELISA KitAnti-Human Hsp70 (IgG/A/M) StressXPress ELISA KitHeme Oxygenase-1 (HO-1), human, StressXPress ELISA KitHeme Oxygenase-1 (HO-1), Rat StressXPress ELISA KitHsp90alpha StressXpress ELISA KitHsp70-A2 Protein - low EndotoxinHsp70-A2 Protein - low EndotoxinHsp60 Protein - low EndotoxinHsp60 Protein - low EndotoxinHsp70 (Hsp72) Protein - low EndotoxinHsp70 (Hsp72) Protein - low EndotoxinHsp65 Protein - low EndotoxinHsp65 Protein - low EndotoxinHsp27 - low EndotoxinHsp27 - low EndotoxinHsp60 (Mouse) - low EndotoxinHsp60 (Mouse) - low Endotoxin17-AAGGeldanamycinHeLa Cell Lysate, Heat ShockedHsp25 ProteinHsp25 ProteinHsp47 (Colligin) ProteinHsp47 (Colligin) ProteinHsp60 ProteinHsp60 ProteinHO-2 (Heme Oxygenase-2) ProteinHO-2 (Heme Oxygenase-2) ProteinHSP70 (Hsp72) ProteinHSP70 (Hsp72) ProteinAnti-HO-1, clone HO-1-1Anti-HO-1, clone HO-1-1Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, Biotin ConjugateAnti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, Biotin ConjugateAnti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2Anti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, FITC conjugatedAnti-HO-1 (Heme Oxygenase, Hsp32), clone HO-1-2, FITC conjugatedAnti-HO-1 (Heme Oxygenase-1, Hsp32)Anti-HO-2 (Heme Oxygenase-2)Anti-HO-2 (Heme Oxygenase-2)Anti-Cpn10Anti-Cpn10Anti-GroESAnti-GroES
Cat. No. Product Size Price E
Heat Shock Proteins and Molecular Chaperones Price List
SPA-221DSPA-221FSPA-222DSPA-222FSPA-223DSPA-223FSPA-224DSPA-224FSPA-225CSPA-225ESPA-226CSPA-226ESPA-227CSPA-227ESPA-230DSPA-230FSPA-240DSPA-240FSPA-400CSPA-400ESPA-410DSPA-410FSPA-450ESPA-470DSPA-470FSPA-523DSPA-523FSPA-523PUCSPA-523PUESPA-524DSPA-524FSPA-524PUCSPA-524PUESPA-525CSPA-525ESPA-585CSPA-585ESPA-600DSPA-600FSPA-601DSPA-601FSPA-670CSPA-670ESPA-725CSPA-725ESPA-754ESPA-756DSPA-757CSPA-757ESPA-766CSPA-766ESPA-796ESPA-800BDSPA-800BFSPA-800FIDSPA-800FIFSPA-801ESPA-803DSPA-803FSPA-806DSPA-806FSPA-807DSPA-807FSPA-810APDSPA-810APFSPA-810BDSPA-810BFSPA-810D
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173365175372173365160355154345154345154345175372173365199421188428368207450207421170375199409170375207421150338161355182399140318150338451464148299148331344187395187395355161355160356182394228470220463207
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Anti-alpha A CrystallinAnti-alpha A CrystallinAnti-alpha B Crystallin, clone 1B6.1-3G4Anti-alpha B Crystallin, clone 1B6.1-3G4Anti-alpha B CrystallinAnti-alpha B CrystallinAnti-alpha A/alpha B-CrystallinAnti-alpha A/alpha B-CrystallinAnti-phospho-Crystallin, alphaB (Ser19)Anti-phospho-Crystallin, alphaB (Ser19)Anti-phospho-Crystallin, alphaB (Ser45)Anti-phospho-Crystallin, alphaB (Ser45)Anti-phospho-Crystallin, alphaB (Ser59)Anti-phospho-Crystallin, alphaB (Ser59)Anti-beta-Crystallin, clone 3.H9.2Anti-beta-Crystallin, clone 3.H9.2Anti-GrpEAnti-GrpEAnti-Hsp40 (Heat Shock Protein 40, HDJ1)Anti-Hsp40 (Heat Shock Protein 40, HDJ1)Anti-DnaJAnti-DnaJAnti-Hsp40 (Heat Shock Protein 40, HDJ1), clone 2E1Anti-Hsp47 (Colligin), clone M16.10A1Anti-Hsp47 (Colligin), clone M16.10A1Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser78) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser82)Anti-phospho-Hsp27 (Ser82)Anti-phospho-Hsp27 (Ser82) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser82) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser15) (Heat Shock Protein 27)Anti-phospho-Hsp27 (Ser15) (Heat Shock Protein 27)Anti-ERp57 (Grp58)Anti-ERp57 (Grp58)Anti-CalreticulinAnti-CalreticulinAnti-Calreticulin, clone FMC75Anti-Calreticulin, clone FMC75Anti-p23Anti-p23Anti-Erp57, clone MaP.Erp57Anti-Erp57, clone MaP.Erp57Anti-Hsp70B (Heat Shock Protein 70B), clone 165fAnti-Hsp70B (Heat Shock Protein 70B)Anti-Hsp70, Hsc70 (Heat Shock Protein 70, Heat Shock Cognate Protein 70)Anti-Hsp70, Hsc70 (Heat Shock Protein 70, Heat Shock Cognate Protein 70)Anti-HipAnti-HipAnti-Hsp20 (Heat Shock Protein 20)Anti-Hsp27 (Heat Shock Protein 27), Biotin conjugate, clone G3.1Anti-Hsp27 (Heat Shock Protein 27), Biotin conjugate, clone G3.1Anti-Hsp27 (Heat Shock Protein 27), clone G3.1, FITC conjugatedAnti-Hsp27 (Heat Shock Protein 27), clone G3.1, FITC conjugatedAnti-Hsp25 (Heat Shock Protein 25)Anti-Hsp27 (Heat Shock Protein 27)Anti-Hsp27 (Heat Shock Protein 27)Anti-Hsp60 (Heat Shock Protein 65), clone LK-1Anti-Hsp60 (Heat Shock Protein 65), clone LK-1Anti-Hsp60 (Heat Shock Protein 65), clone LK-2Anti-Hsp60 (Heat Shock Protein 65), clone LK-2Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, AP-conjugatedAnti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, AP-conjugatedAnti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, Biotin-conjugatedAnti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5, Biotin-conjugatedAnti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5
Cat. No. Product Size Price E
SPA-810FSPA-810FIESPA-810FIHSPA-811DSPA-811FSPA-812CSPA-812ESPA-815APDSPA-815APFSPA-815DSPA-815FSPA-816DSPA-816FSPA-820APDSPA-820APFSPA-820DSPA-820FSPA-822DSPA-822FSPA-826DSPA-826FSPA-827DSPA-827FSPA-828CSPA-828ESPA-829CSPA-829ESPA-830DSPA-830FSPA-835DSPA-835FSPA-840DSPA-840FSPA-842CSPA-842ESPA-843CSPA-843ESPA-845DSPA-845FSPA-846CSPA-846ESPA-860DSPA-860FSPA-865DSPA-865FSPA-890DSPA-890FSPA-891DSPA-891FSPA-895DSPA-895FSPA-896CSPA-896ESPA-897ESPA-901DSPA-901FSPA-950CSPA-950ESPA-960CSPA-960ESPA-1040DSPA-1040FSPA-1101DSPA-1101FSPA-1103DSPA-1103FSPP-225JSPP-225L
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450228470211421211421212493207479212378212493207450207450207450207421144293
35620745019042116135514432214432216135514429321547221547219443019443017939416135543421443414732714732717537217438617438648
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Anti-Hsp70 (Heat Shock Protein, Hsp72), clone C92F3A-5Anti-Hsp70 (Heat Shock Protein 70), clone C92F3A-5, FITC conjugatedAnti-Hsp70 (Heat Shock Protein 70), clone C92F3A-5, FITC conjugatedAnti-Hsp70 (Heat Shock Protein, Hsp72)Anti-Hsp70 (Heat Shock Protein, Hsp72)Anti-Hsp70 (Heat Shock Protein, Hsp72)Anti-Hsp70 (Heat Shock Protein, Hsp72)Anti-Hsc70 (Hsp73), clone 1B5 (Rat), AP-conjugatedAnti-Hsc70 (Hsp73), clone 1B5 (Rat), AP-conjugatedAnti-Hsc70 (Hsp73), clone 1B5 (Rat)Anti-Hsc70 (Hsp73), clone 1B5 (Rat)Anti-Hsc70 (Hsp73)Anti-Hsc70 (Hsp73)Anti-Hsp70/Hsc70, AP conjugateAnti-Hsp70/Hsc70, AP conjugateAnti-Hsp70/Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone N27F3-4Anti-Hsp70/Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone N27F3-4Anti-Hsp70, Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone BB70Anti-Hsp70, Hsc70 (Heat Shock Pro. 70, HS Cognate Pro. 70), clone BB70Anti-Grp78 (BiP)Anti-Grp78 (BiP)Anti-KDEL, clone 10C3Anti-KDEL, clone 10C3Anti-Hsp60 (Heat Shock Protein 60)Anti-Hsp60 (Heat Shock Protein 60)Anti-Hsp60 (Heat Shock Protein 65), clone Mab-11-13Anti-Hsp60 (Heat Shock Protein 65), clone Mab-11-13Anti-Hsp90 (Heat Shock Protein 90), clone AC88Anti-Hsp90 (Heat Shock Protein 90), clone AC88Anti-Hsp90 (Heat Shock Protein 90), clone 16F1Anti-Hsp90 (Heat Shock Protein 90), clone 16F1Anti-Hsp90 alpha, clone 9D2Anti-Hsp90 alpha, clone 9D2Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3705Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3705Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3701Anti-Hsp90 beta (Heat Shock Protein 90b), clone K3701Anti-Hsp90 (Heat Shock Protein 90), clone 2D12Anti-Hsp90 (Heat Shock Protein 90), clone 2D12Anti-Hsp90 (Heat Shock Protein 90)Anti-Hsp90 (Heat Shock Protein 90)Anti-Calnexin-CAnti-Calnexin-CAnti-CalnexinAnti-CalnexinAnti-PDI (Protein Disulfide Isomerase)Anti-PDI (Protein Disulfide Isomerase)Anti-PDI (Protein Disulfide Isomerase), clone 1D3Anti-PDI (Protein Disulfide Isomerase), clone 1D3Anti-HO-1 (Hsp32, Heme Oxygenase-1)Anti-HO-1 (Hsp32, Heme Oxygenase-1)Anti-HO-1 (Hsp32, Heme Oxygenase-1)Anti-HO-1 (Hsp32, Heme Oxygenase-1)Anti-HO-2 (Heme Oxygenase-2)Anti-HSF-1Anti-HSF-1Anti-HSF-1, clone 10H8 (Rat)Anti-HSF-1, clone 10H8 (Rat)Anti-HSF-2, Rat monoclonal IgG 3F2Anti-HSF-2, Rat monoclonal IgG 3F2Anti-Hsp104 (Heat Shock Protein 104)Anti-Hsp104 (Heat Shock Protein 104)Anti-Hsp110/70 (Family)Anti-Hsp110/70 (Family)Anti-Hsp104 (Heat Shock Protein 104)Anti-Hsp104 (Heat Shock Protein 104)Crystallin, alphaCrystallin, alpha
Cat. No. Product Size Price E
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[email protected] · www.biomol.deTechnischer Support: [email protected]
discontinued
Heat Shock Proteins and Molecular Chaperones Price List
SPP-226BSPP-226FSPP-227BSPP-227FSPP-400BSPP-400ESPP-610CSPP-610GSPP-620CSPP-620ESPP-620FSPP-640DSPP-640FSPP-650CSPP-650ESPP-650FSPP-715FSPP-730DSPP-730FSPP-732BSPP-732ESPP-741BSPP-741DSPP-741FSPP-742BSPP-742ESPP-751DSPP-751FSPP-752BSPP-752ESPP-758BSPP-758ESPP-762BSPP-762ESPP-765BSPP-765ESPP-767ESPP-770BSPP-770ESPP-776DSPP-776FSPP-900BSPP-900ESPS-771DSPS-771FSPS-825DSPS-870DSPS-870FSPS-875DSPS-875FSRA-1400DSRA-1400FSRA-1500DSRA-1500FSRP-1510BSRP-1510EVAA-PT048CVAA-PT048EVAM-PT046CVAM-PT046EVAM-SV021CVAM-SV021EVAP-PT068CVAP-PT068EVAP-SV003D
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114356114356207450144208148287434499
1272148217364479349799212434228299887221479254699144355228492179479136378421177432179421212434161355421156348175396228399173365199409199390173365160355173365372
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Crystallin, alphaACrystallin, alphaACrystallin, alphaBCrystallin, alphaBHsp40 ProteinHsp40 ProteinGroEL ProteinGroEL ProteinGroES ProteinGroES ProteinGroES ProteinDnaJ ProteinDnaJ ProteinGrpE ProteinGrpE ProteinGrpE ProteinHsp27 ProteinHO-1 (Hsp32, Heme Oxygenase-1)HO-1 (Hsp32, Heme Oxygenase-1)HO-1 (Hsp32, Heme Oxygenase-1) ProteinHO-1 (Hsp32, Heme Oxygenase-1) ProteinHsp60 ProteinHsp60 ProteinHsp60 ProteinHsp60 ProteinHsp60 ProteinHsc70 (Hsp73) Active ProteinHsc70 (Hsp73) Active ProteinHsc70 (Hsp73) Protein-ATPase FragmentHsc70 (Hsp73) Protein-ATPase FragmentHsp70 Protein, ratHsp70 Protein, ratHsp70B‘ ProteinHsp70B‘ ProteinGrp78 (BiP) ProteinGrp78 (BiP) ProteinHip ProteinHsp90 ProteinHsp90 ProteinHsp90 alpha ProteinHsp90 alpha ProteinHSF-1 ProteinHSF-1 ProteinAnti-Hsp90 alphaAnti-Hsp90 alphaAnti-Grp75, clone 30A5Anti-GroEL, clone 9A1/2Anti-GroEL, clone 9A1/2Anti-GroELAnti-GroELAnti-FKBP59 (Hsp56, p59), clone KN382/EC1Anti-FKBP59 (Hsp56, p59), clone KN382/EC1Anti-Hop (p60), clone DS14F5Anti-Hop (p60), clone DS14F5HOP (p60) ProteinHOP (p60) ProteinAnti-KDEL Receptor, clone KR-10Anti-KDEL Receptor, clone KR-10Anti-Membrin, clone 4HAD6Anti-Membrin, clone 4HAD6Anti-rSec6, clone 9H5Anti-rSec6, clone 9H5Anti-UGGTAnti-UGGTAnti-Cysteine String Protein (CSP)
Cat. No. Product Size Price E
Alle Preise zzgl. MwSt. und Versandkosten.Preisänderungen und Irrtümer vorbehalten. 06/2007
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