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Home / Primary Antibodies / Monoclonal Antibodies

HSP90 Antibody, Clone D7A - SMC-137

BHA11900520
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Email
[email protected]
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Swissprot P11501
Accession Number NP_001103255.1
Gene Id 9031
Target HSP90
Clone No D7A
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Tumor Biomarkers, Protein Trafficking
Buffer PBS pH7.2, 50% glycerol, 0.09% sodium azide
Concentration 1 mg/ml
Dilutions WB (1:500), IP (5µg) ; optimal dilutions for assays should be determined by the user.
Purification Protein G Purified
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).
Shipping Temperature Blue Ice or 4°C
Specificity Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37.
Storage -20ÂşC
Storage Buffer PBS pH7.2, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Storage Temperature -20°C
Applications AM, ELISA, IHC, IP, WB
Description WB ; IHC ; IP ; ELISA ; AM
Dilution WB (1:500), IP (5ug) ; optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 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.
Combination SKU Supplier No. Conjugate Size Your price Quantity
BHA11900520-1 SMC-137D Unconjugated 100 ug $345
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BHA11900520-2 SMC-137C Unconjugated 25 ug $161
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BHA11900520-3 SMC-137D-A390 ATTO 390 100 ug $399
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BHA11900520-4 SMC-137D-A488 ATTO 488 100 ug $398
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BHA11900520-5 SMC-137D-A594 ATTO 594 100 ug $398
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BHA11900520-6 SMC-137D-ALP Alkaline Phosphatase 100 ug $392
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BHA11900520-7 SMC-137D-APC APC 100 ug $397
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BHA11900520-8 SMC-137D-BI Biotin 100 ug $394
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BHA11900520-9 SMC-137D-FITC FITC 100 ug $389
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BHA11900520-10 SMC-137D-HRP HRP 100 ug $385
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BHA11900520-11 SMC-137D-PCP PerCP 100 ug $397
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BHA11900520-12 SMC-137D-RPE RPE 100 ug $395
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BHA11900520-13 SMC-137S Unconjugated 12 ug $44
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