Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) (AA 185-335) antibody

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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
AA 185-335
(3), (3), (2)
(2), (1)
Clonality (Clone)
Monoclonal ()
ELISA, Immunohistochemistry (IHC), Western Blotting (WB)
(3), (3), (3), (2), (2), (2)
Pubmed 9 references available
Quantity 100 μg
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Immunogen Recombinant human HSP90beta, Specificity mapped to amino acids 185-335
Clone Hyb-K3701
Specificity Detects 90 kDa. This is a beta specific product, does not cross-react with alpha isoforms.
Sensitivity 1 µg/ml was sufficient for detection of Hsp90beta in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
Purification Protein G Purified
Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85 % sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer.(2) From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, HSP90 is highly conserved between species, having 60 % and 78 % amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 (9).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Research Area Signaling, Heat Shock Proteins, Cancer
Application Notes Recommended Dilution: WB (1:1000), IHC (1:3000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Image no. 1 for anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) (AA 185-335) antibody (ABIN361720) Hsp90beta (K3701), cell lines.
Product cited in: Muralidharan, Ambade, Fulham et al.: "Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, 2014 (PubMed).

Bates, Salzman, May et al.: "Extensive gene-specific translational reprogramming in a model of B cell differentiation and Abl-dependent transformation." in: PLoS ONE, Vol. 7, Issue 5, pp. e37108, 2012 (PubMed).

Background publications Kishimoto, Fukuma, Mizuno et al.: "Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones." in: Cell stress & chaperones, Vol. 10, Issue 4, pp. 296-311, 2005 (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).

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

Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (PubMed).

Lowe: "Colipase stabilizes the lid domain of pancreatic triglyceride lipase." in: The Journal of biological chemistry, Vol. 272, Issue 1, pp. 9-12, 1997 (PubMed).

Whitesell, Mimnaugh, De Costa et al.: "Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 18, pp. 8324-8, 1994 (PubMed).

Catalog No. ABIN361720
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