HSP90AA1 Antibody – Mouse Monoclonal

Background Info: Recognizes 90kDa proteins corresponding to the molecular mass of Hsp90. Hsp90alpha specific for human samples. Can isolate complexes of Hsp90, Src kinase and cec37.

Scientific Background: 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 (4-7). Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% 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 (8-9). The number of proteins now known 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(6). 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 immune-adsorption 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 (10).

1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296. 2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880. 3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19. 4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186. 6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 8. Pratt W, Toft D. (1997) Endocr Rev 18: 306-360. 9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420-434. 10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324- 8328.

Small volumes of anti-HSP90AA1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS800378 is an antibody targeting HSP90AA1. Also known as Hsp90 Antibody: PerCP. Reactive in Bovine, Chicken, Human, Mouse, Porcine (Pig), Rat, Rabbit. Host: Mouse.