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Please feel free to continue placing orders via our website or via fax at 734-971-3640. You may send an email to customer service at custserv@caymanchem.com , or to technical support at techserv@caymanchem.com which we will respond to the next business day. Cayman will resume regular business hours and shipping schedules on Tuesday, May 29, 2012. Thank you for your patience and understanding.
Hsp90β Polyclonal AntibodyCayman Chemical Item Number 19612 Heat Shock Protein 90β
Description
Antigen:
Full length Hsp90
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Host:
rabbit
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Application(s):
WB, ELISA, and IP
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Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, Hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex.1,2,3,4 Despite its label of being a heat shock protein, Hsp90 is one of the most highly expressed proteins in unstressed cells (1-
1 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). 2 Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001). 3 Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).
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Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70- 5 Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).
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Pratt, W.B. The Hsp90-
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Whitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90-
Background ReadingWhitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90- Pratt, W.B. The Hsp90- Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997). Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70- Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001). Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002). 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). Show all 7 Hide all but first 3 |
This product is available in custom sizes and/or larger quantities. Please contact our Sales Department for a quote or to purchase. Pricing updated 2012-05-26. Prices are subject to change without notice. To ask for assistance with one of our products please contact a Technical Support Scientist. Warning This product is not for human or veterinary use. Related ProductsShow all 16 Hide all but first 3Downloads
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Cayman Chemical is a manufacturer, supplier and vendor of biochemical reagents, assay kits, antibodies, and proteins. |
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Cayman Chemical Company · 1180 East Ellsworth Road · Ann Arbor, Michigan 48108 · USA
Toll Free: (800) 364-9897 (USA and Canada Only) · Fax: (734) 971-3640
Copyright 2012 Cayman Chemical Company
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