| References |
| Synonyms |
|
| Formula Weight |
90.0 |
| Formulation |
Protein G affinity-purified mouse IgG at a protein concentration of 1 mg/ml in PBS, pH. 7.2, containing 50% glycerol and 0.09% sodium azide |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human (β-specific) Hsp90β |
+ |
| Rabbit (β-specific) Hsp90β |
+ |
| Chicken (α/β) Hsp90β |
+ |
| Rat Hsp90β |
+ |
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|
Background Reading
Loo, M.A., Jensen, T.J., Cui, L., et al. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by proteasome. EMBO J 17(23) 6879-6887 (1998).
Nemoto, T., Sato, N., Iwanari, H., et al. Domain structures and immunogenic regions of the 90-kDa heat shock protein (Hsp90). Probing with a library of anti-Hsp90 monoclonal antibodies and limited proteolysis. J Biol Chem 272(42) 26179-26187 (1997).
Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).
Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).
Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).
Whitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91 8324-8328 (1994).
Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).
Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).
Barent, R.L., Nair, S.C., Carr, D.C., et al. Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes. Mol Endocrinol 12 342-354 (1998).
Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).
Minami, Y., Kawasaki, H., Miyata, Y., et al. Analysis of native forms and isoforms compositions of the mouse 90-kDa heat shock protein, Hsp90. J Biol Chem 266(16) 10099-10103 (1991).
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| Size |
Global Purchasing |
| 50 µg |
|
| 200 µg |
|
Description
Antigen:
human recombinant Hsp90β
·
Clone designation:
H90-10
·
Host:
mouse
·
Isotype:
IgG2α
·
Application(s):
WB, IP, and EIA
·
Hsp90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of Hsp90, are expressed in the cytosolic compartment.1 Despite the similarities, Hsp90α exists predominantly as a homodimer, while Hsp90β exists mainly as a monomer.2 From a functional perspective, Hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex.3,4,5,6 Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acids similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a heat shock protein, Hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the Hsp90 - regulated proteins that have been discovered to date are involved in cell signalling.7,8 The number of proteins now known to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5
1
Nemoto, T., Sato, N., Iwanari, H., et al. Domain structures and immunogenic regions of the 90-kDa heat shock protein (Hsp90). Probing with a library of anti-Hsp90 monoclonal antibodies and limited proteolysis. J Biol Chem 272(42) 26179-26187 (1997).
2
Minami, Y., Kawasaki, H., Miyata, Y., et al. Analysis of native forms and isoforms compositions of the mouse 90-kDa heat shock protein, Hsp90. J Biol Chem 266(16) 10099-10103 (1991).
3
Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).
4
Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).
5
Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).
6
Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).
7
Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).
8
Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).
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