Technical Data
H1834-55A1
Heat Shock Protein 90, alpha (HSP90a)
Description:
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment. Despite the similarities, HSP90 exists predominantly as a homodimer while HSP90b exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. Furthermore, Hsp90 is highly conserved between species; having 60% and 78% amino acid 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 (12% 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 signaling. The number of proteins now know 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 When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function.

Applications:
Suitable for use in Western Blot, ELISA, Immunoprecipitation and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 1ug/ml for detection in 20ug of HeLa lysate.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG2a7L17Affinity Purified
SizeStorageShippingSourceHost
25ug-20CBlue IceHumanMouse
Concentration:
~1mg/ml
Immunogen:
Recombinant human HSP90 alpha
Purity:
Purified by Protein G affinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide, 50% glycerol.
Specificity:
Recognizes human HSP90 alpha at ~90kD. Does not crossreact with HSP90 beta. Species Crossreactivity: rat
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Nemoto, T. et al. (1997) J.Biol Chem. 272, 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266, 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278, 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59,157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18,306360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217, 420434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91, 83248328. 10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5), 881-889.