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Home / Primary Antibodies / Polyclonal Antibodies

Rabbit Anti-Human HSP90 Polyclonal (SPC-104)

BHA11906284
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Email
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Antigen HSP90
Swissprot P08238
Accession Number NP_031381.2
Gene Id 3326
Target HSP90
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Tumor Biomarkers, Protein Trafficking
Buffer PBS pH 7.4, 50% glycerol, 0.09% sodium azide
Concentration 1 mg/ml
Dilutions WB (1:500), IHC (1:100), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Purification Protein A 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 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). Looking for more information on HSP90 Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Shipping Temperature Blue Ice or 4°C
Specificity Detects ~90kDa.
Storage -20ºC
Storage Buffer PBS pH 7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Storage Temperature -20°C
Applications ELISA, IHC, IP, WB, ICC/IF
Description WB ; IHC ; ICC ; IF ; IP ; ELISA
Dilution WB (1:500), IHC (1:100), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 1. Arlander S.J.H., 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 W.B. (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
BHA11906284-1 SPC-104D Unconjugated 100 ul $283
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BHA11906284-2 SPC-104D-A390 ATTO 390 100 ul $338
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BHA11906284-3 SPC-104D-A488 ATTO 488 100 ul $337
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BHA11906284-4 SPC-104D-A594 ATTO 594 100 ul $337
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BHA11906284-5 SPC-104D-APC APC 100 ul $336
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BHA11906284-6 SPC-104D-BI Biotin 100 ul $333
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BHA11906284-7 SPC-104D-FITC FITC 100 ul $327
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BHA11906284-8 SPC-104D-HRP HRP 100 ul $323
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BHA11906284-9 SPC-104D-PCP PerCP 100 ul $336
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BHA11906284-10 SPC-104D-RPE RPE 100 ul $334
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BHA11906284-11 SPC-104S Unconjugated 12 ul $45
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