Mouse Monoclonal to Hsp90 alpha,beta
MBH90AB (IgG1)
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Product No. |
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11-533-C025 |
purified |
0.025 mg |
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choose region |
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11-533-C100 |
purified |
0.1 mg |
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Background
Hsp90 (heat shock protein 90) is one of the most abundant chaperones in the cytosol of eukaryotic cells. It interacts with various proteins, including protein kinases and transcription factors, and either facilitates their stabilization and activation or directs them for proteasomal degradation. Hsp90 thus affects multiple signaling pathways and biological processes and modulation of this single target offers the prospect of simultaneous intervence to various key points of oncogenic transformation. Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. There are two isoforms, alpha and beta, of vertebrate Hsp90. Whereas Hsp90 beta is expressed constitutively to a high level, Hsp90 alpha is stress-inducible and is overexpressed in many cancerous cells.
Entrez Gene (HSP90A, human):
14q32.33Entrez Gene (HSP90B, human):
6p12
Specificity
The antibody MBH90AB recognizes the epitope EEEVE within N-terminal part of ubiquitously expressed Hsp90 alpha and Hsp90 beta proteins with calculated Mw of 84.7 kDa and 83.3 kDa, respectively, however, migrating as 90 kDa bands under reducing SDS-PAGE conditions.
Immunogen
Peptide corresponding to the sequence EEVHHGEEEVEC within N-terminal part of human Hsp90.
Species Reactivity:
- Human
- Mouse
- Bovine
- Other not determined
Negative Species:
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Applications:
Usage note: Indicated dilutions are recommended starting points for use of this product. Working concentrations should be determined by the investigator.
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General references
*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. 1998 Apr;217(4):420-34.
[Abstract]
*Scheibel T, Buchner J.: The Hsp90 complex--a super-chaperone machine as a novel drug target. Biochem Pharmacol. 1998 Sep 15;56(6):675-82.
[Abstract]
*Hooven TA, Yamamoto Y, Jeffery W.R.: Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis. Int J Dev Biol. 2004;48(8-9):731-8.
[Abstract]
*Millson SH, Truman AW, Rácz A, Hu B, Panaretou B, Nuttall J, Mollapour M, Söti C, Piper P.W.: Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol. FEBS J. 2007 Sep;274(17):4453-63.
[Abstract]
*Pearl LH, Prodromou C, Workman P.: The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J. 2008 Mar 15;410(3):439-53.
[Abstract]
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For research use only. Not for drug, diagnostic or other use.
Related Products
Mouse IgG1 Isotype Control
Example Data

Fig. 1.
Fig. 1. Western blotting analysis of Hsp90
alpha and beta protein by antibody
MBH90AB to both Hsp90
alpha and beta isoform.