Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody

Details for Product No. ABIN264895
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Antigen
Synonyms hsp90b, HSP90-BETA, HSP90B, HSPC2, Hspcb, 90kDa, AL022974, C81438, Hsp84, Hsp84-1, Hsp90, hsp90beta, wu:fa29f01, wu:fa91e11, wu:fd59e11, wu:gcd22h07, HSPCB, D6S182, HSP84, HSP90
Reactivity
Human, Mouse (Murine), Rat (Rattus)
(207), (124), (112), (20), (19), (19), (16), (12), (9), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Host
Rabbit
(152), (65), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (Frozen Sections) (IHC (fro)), Enzyme Immunoassay (EIA), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
(202), (95), (83), (67), (44), (39), (34), (18), (14), (14), (12), (10), (1), (1), (1), (1)
Pubmed 5 references available
Quantity 0.1 mL
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Catalog No. ABIN264895
324.50 $
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Immunogen Purified recombinant Human HSP90 beta
Isotype IgG
Specificity This antibody ist specific for Hsp90 beta and does not cross react with Hsp90 alpha.
Purification Serum
Alternative Name HSP90AB1 / HSP90 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).Synonyms: HSP84, HSP90B, HSPC2, HSPCB, Heat shock 84 kDa, Heat shock protein HSP 90-beta
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Application Notes Western blot (1): 1: 20000-40000 (ECL). ELISA. IP. Immunohistochemistry.
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.
Supplier Images
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (2) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (Image 2)
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (3) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) 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).

Orthwein, Patenaude, Affar et al.: "Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90." in: The Journal of experimental medicine, Vol. 207, Issue 12, pp. 2751-65, 2010 (PubMed).

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