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Home / Primary Antibodies / Monoclonal Antibodies

HSP90 Antibody, Clone AC-16 - SMC-112

BHA11900181
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+1 866.986.9598
Email
[email protected]
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Swissprot Q8LLI5
Accession Number AAM90675.1
Gene Id 4768
Target HSP90
Clone No AC-16
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Tumor Biomarkers, Protein Trafficking
Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration 1 mg/ml
Dilutions WB (1:1000), IHC (1:2000); 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 (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 immuno-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 (7).
Shipping Temperature Blue Ice or 4°C
Specificity Detects 90kDa. 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.
Storage -20ºC
Storage Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Storage Temperature -20°C
Applications AM, IHC, WB
Description WB ; IHC ; AM
Dilution WB (1:1000), IHC (1:2000); optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 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.
Combination SKU Supplier No. Conjugate Size Your price Quantity
BHA11900181-1 SMC-112B Unconjugated 200 ug $345
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BHA11900181-2 SMC-112A Unconjugated 50 ug $161
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BHA11900181-3 SMC-112B-A390 ATTO 390 200 ug $448
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BHA11900181-4 SMC-112B-A488 ATTO 488 200 ug $444
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BHA11900181-5 SMC-112B-A594 ATTO 594 200 ug $444
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BHA11900181-6 SMC-112B-ALP Alkaline Phosphatase 200 ug $432
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BHA11900181-7 SMC-112B-APC APC 200 ug $443
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BHA11900181-8 SMC-112B-BI Biotin 200 ug $435
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BHA11900181-9 SMC-112B-FITC FITC 200 ug $427
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BHA11900181-10 SMC-112B-HRP HRP 200 ug $419
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BHA11900181-11 SMC-112B-PCP PerCP 200 ug $443
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BHA11900181-12 SMC-112B-RPE RPE 200 ug $437
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BHA11900181-13 SMC-112S Unconjugated 12 ug $44
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