Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody

Details for Product No. ABIN264851
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Human, Mouse (Murine), Rat (Rattus)
(15), (9), (8), (7), (4), (4), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1)
(14), (5), (2)
Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunohistochemistry (Frozen Sections) (IHC (fro)), ELISA, Immunoprecipitation (IP), Western Blotting (WB)
(21), (9), (8), (6), (4), (3), (2), (1), (1), (1)
Pubmed 7 references available
Catalog no. ABIN264851
Quantity 25 µL
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Immunogen Full length Human protein Hsp90
Specificity Detects ~90kDa proteins corresponding to the molecular mass of HSP90alphabeta.
Purification Serum
Alternative Name Heat Shock Protein 90 (HSP90) alpha/beta
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).
Alternate names: HSP-84, HSP-84, HSP-86, HSP-86, HSP-90, HSP84, HSP84, HSP86, HSP86, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSPC1, HSPC2, HSPCA, HSPCB, Heat shock protein HSP 90-alpha, Heat shock protein HSP 90-beta, Renal carcinoma antigen NY-REN-38
Gene ID 3326
NCBI Accession NP_031381.2
UniProt P08238
Application Notes Western blot (1): 1: 20000-40000 (ECL). ELISA. Immonoprecipitation. Immunohistochemistry on frozen sections. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
Expiry Date 12 months
Supplier Images
anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody
anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody (2) anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody (Image 2)
anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody (3) anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) antibody (Image 3)
Background publications Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (PubMed).

Pratt: "The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors." in: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), Vol. 217, Issue 4, pp. 420-34, 1998 (PubMed).

Pearl, Prodromou: "Structure, function, and mechanism of the Hsp90 molecular chaperone." in: Advances in protein chemistry, Vol. 59, pp. 157-86, 2002 (PubMed).

Arlander, Eapen, Vroman et al.: "Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress." in: The Journal of biological chemistry, Vol. 278, Issue 52, pp. 52572-7, 2003 (PubMed).

Marubayashi, Koppikar, Taldone et al.: "HSP90 is a therapeutic target in JAK2-dependent myeloproliferative neoplasms in mice and humans." in: The Journal of clinical investigation, Vol. 120, Issue 10, pp. 3578-93, 2010 (PubMed).

Wagatsuma, Shiozuka, Kotake et al.: "Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells." in: Molecular and cellular biochemistry, Vol. 358, Issue 1-2, pp. 265-80, 2011 (PubMed).

Verheyen, Peeraer, Nuydens et al.: "Systemic anti-vascular endothelial growth factor therapies induce a painful sensory neuropathy." in: Brain : a journal of neurology, Vol. 135, Issue Pt 9, pp. 2629-41, 2012 (PubMed).

Hosts (14), (5), (2)
Reactivities (15), (9), (8), (7), (4), (4), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1)
Applications (21), (9), (8), (6), (4), (3), (2), (1), (1), (1)
Epitopes (2), (2)
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