HSP90AB1 Antibody – Mouse Monoclonal

Background Info: Immunoprecipitates 90kDa proteins corresponding to the molecular mass of Hsp90. Co-immunoprecipitates Hsp90 complexes, including Hsp70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2alpha (eIF-2alpha) kinase (HRI).

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 (1-4). 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 (5-6). 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 (7).

1. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 2. Pearl H, et al. (2001) Adv Protein Chem 59:157-186. 3. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 4. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 5. Pratt W, Toft D. (1997) Endocr Rev 18: 306-360. 6. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420-434. 7. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324- 8328. 8. Perdew, G. H. (1988) JBC 263 (27): 13802-13805 9. Dalman, F. C. et al.(1989) JBC 264(33): 19815-19821 10. Uma, S. et al. (1997) JBC 272(17): 11648-11656.
1. Ardi, V.C., Alexander, L.D., Johnson, V. and McAlpine S.R. (2011). Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins. ACS Chem Biol. 6 (12), 1357-1366. doi: 10.1021/cb200203m

Small volumes of anti-HSP90AB1 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.

MBS803879 is an antibody targeting HSP90AB1. Also known as Hsp90 complex Antibody: FITC. Reactive in Human, Mouse, Rat, Rabbit. Host: Mouse.