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).
HSP90AA1, HSPN, LAP2, HSP86, HSPC1, HSPCA, Hsp89, Hsp90, HSP90N, HSPCAL1, HSPCAL4, FLJ31884
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.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. 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.
Dolan Maureen et al., Tools of the Trade: Developing Antibody-Based Detection Capabilities for Recombinant Proteins Methods Mol Biol. July 2005 10.1007/978-1-61779-433-9_4
Medrano Giuliana et al., Quality Assessment of Recombinant Proteins Produced in Plants Recombinant Gene Expression January 2012 10.1007/978-1-61779-433-9_29
Kostenko Sergiy et al., Phosphorylation of heat shock protein 40 (Hsp40/DnaJB1) by mitogen-activated protein kinase-activated protein kinase 5 (MK5/PRAK) The International Journal of Biochemistry & Cell Biology February 2014 10.1016/j.biocel.2013.11.004
Cancer, Cellular Stress, p38 Pathway