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

Details for Product No. ABIN263957
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Human, Rat (Rattus), Yeast (Saccharomyces cerevisiae)
(35), (10), (9), (4), (4), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1)
(31), (6), (2)
Clonality (Clone)
Monoclonal ()
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Immunohistochemistry (Frozen Sections) (IHC (fro)), ELISA, Western Blotting (WB)
(39), (25), (23), (10), (5), (4), (3), (2), (1), (1), (1)
Pubmed 8 references available
Quantity 0.1 mg
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Catalog No. ABIN263957
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Immunogen Recombinant Human hsp90 alpha
Clone Hyb-K41220A
Isotype IgG2a
Characteristics Synonyms: HSP90AB1, HSP90B, HSPC2, HSPCB, HSP84, HSP-90, HSP-84, Heat shock protein HSP90-beta, HSP90AA1, HSP90A, HSPC1, HSPCA, HSP86, HSP-86, Renal carcinoma antigenNY-REN-38, Heat shock protein HSP 90-alpha
Purification Affinity Chromatography on Protein G
Alternative Name Heat Shock Protein 90 (HSP90) alpha/beta
Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understoodto 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 thesimilarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly asa monomer. (2) From a functional perspective, hsp90 participates in the folding, assembly,maturation, and stabilization of specific proteins as an integral component of a chaperonecomplex. (3-6) Furthermore, Hsp90 is highly conserved between species, having 60% and78% amino acid similarity between mammalian and the corresponding yeast andDrosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryoticcells. Despite its label of being a heat-shock protein, hsp90 is one of the most highlyexpressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a numberof housekeeping functions – including controlling the activity, turnover, and trafficking of avariety of proteins. Most of the hsp90-regulated proteins that have been discovered todate are involved in cell signaling (7-8). The number of proteins now know to interact withHsp90 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 thehepatitis B virus and telomerase. 5 When bound to ATP, Hsp90 interacts withco-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming acomplex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexeswith it. In a number of cases, variations in hsp90 expression or hsp90 mutation has beenshown to degrade signaling function via the protein or to impair a specific function of theprotein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such asgeldanamycin and radicicol, inhibit hsp90 function (9).
Gene ID 3320
UniProt P07900
Application Notes ELISA. (Ref.1)Western blot: 1 µg/ml was sufficient for detection of Hsp90alpha/beta by Western Blot in20 µg of HeLa lysate. (Ref.1, 10)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
Concentration 1.0 mg/mL
Buffer PBS, pH 7.2 0.09% Sodium Azide 50% Glycerol
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 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch.
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
Background publications Garg, Hassid: "Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism." in: The Journal of biological chemistry, Vol. 266, Issue 1, pp. 9-12, 1991 (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).

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).

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).

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).

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