抗Hsp90モノクローナル抗体(Anti-Hsp90) Hsp90 antibody (AC-16:クローン名) | StressMarq Biosciences

IHC staining of inflammatory cells and epithelia mucosa in mouse colon tissues.

Hsp90 Antibody

Monoclonal

Anti-Hsp90

Chaperones, Heat Shock, Trafficking

Hsp84, Hsp86, Hsp90, Hsp89, Hsp90Beta, Hsp90A, Hsp90AA1, Hsp90AB1, Hsp90B, Hsp90N, HspC1, HspC2, HspCA, HspCAL1, HspCAL4, HspCB, HspN, LAP2

AC-16

Mouse

IgG2b

Heat shock protein 90 from the water mold Achyla ambisexualis

WB, IHC

Human, Rabbit, Rat, Mouse, Chicken, Achyla, Wheat Germ, Sf9 cell line

AAM90675.1

4768

Q8LLI5

This antibody is reactive with both the constitutive and the inducible form of Hsp90. It does not bind to the native form and does not recognize Hsp90 from E.coli or yeast.

1µg/ml was sufficient for detection of hsp90 by Western Blot in 20µg of HeLa lysate.

Protein G Purified

PBS pH7.4, 50% glycerol, 0.09% sodium azide

1 µg/mL of SMC-112 was sufficient for detection of Hsp90 in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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.