Description: Recombinant full-length human HSP90 alpha was expressed by baculovirus in Sf9 insect cells using a C-terminal His tag.

Storage, Stability, and Shipping: Store product at –70^oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Applications: Western Blot

Molecular Weight: ~94 kDa

Gene Aliases: HSP90AA1, HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90N, HSPCAL1, HSPCAL4, FLJ31884

Scientific Background: HSP90α is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins (1). HSP90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL and mutated p53. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2).

References: 
1. Csermely, P. et al: The 90-kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol Ther. 1998 Aug;79(2):129-68.

2. Eustace, B. K. et al:Functional proteomic screens reveal an essential extracellular role for hsp90-alpha in cancer cell invasiveness. Nature Cell Biol. 6: 507-514, 2004.

		Purity:  Sample Purity Data. For specific information on a given lot, see related technical data sheet.

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