抗Hsp90 complexモノクローナル抗体(Anti-Hsp90 complex) Hsp90 complex antibody (8D3:クローン名) | StressMarq Biosciences

Hsp90 complex isolation (IP) from rabbit reticulocyte lysate (8D3), SDS PAGE.

Hsp90 (complex) Antibody

Monoclonal

Anti-Hsp90 complex

Chaperones, Heat Shock, Trafficking

Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB, Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB

8D3

Mouse

IgM

Ah receptor (Aryl hydrocarbon receptor)

IP

Human, Mouse, Rat, Rabbit. Other species not yet tested.

NP_031381.2

3326

P08238

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 2α (eIF-2α) kinase (HRI).

Best results for IP associated with use of goat anti-mouse IgM beads.

PEG Purified

PBS, 50% glycerol, 0.09% sodium azide

Goat anti-mouse IgM was used to bind 25 µl of protein G-Sepharose. SMC-109 IgM from 0.5 ml of high speed supernatant medium was loaded onto the IgG resin and incubated with 100 µl of rabbit reticulocyte lysate for 30 min. at 30C. After washing (4X1 ml), bound proteins were resolved on SDS PAGE, including hsp90, hsp70 and Hop.

Research 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).

References
1. Arlander SJH, . (2003) 278: 52572-52577.

2. Pearl H, . (2001) 59:157-186.

3. Neckers L, . (2002) 8:S55-S61.

4. Pratt W, Toft D. (2003) 228:111-133.

5. Pratt W, Toft D. (1997) 18: 306–360.

6. Pratt WB. (1998) 217: 420–434.

7. Whitesell L, . (1994) 91: 8324– 8328.

8. Perdew, G. H. (1988) 263 (27): 13802-13805

9. Dalman, F. C. . (1989) 264(33): 19815-19821

10. Uma, S. (1997) 272(17): 11648-11656.

Cited References
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. . 6 (12), 1357-1366.