Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) (AA 291-304) antibody

Details for Product No. ABIN361716
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Antigen
Epitope
AA 291-304
(18), (2)
Reactivity
Human, Rat (Rattus), Yeast (Saccharomyces cerevisiae), Schizosaccharomyces pombe
(34), (10), (9), (4), (4), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Host
Mouse
(30), (6), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), ELISA, Immunohistochemistry (IHC)
(38), (25), (22), (9), (5), (5), (3), (2), (1), (1), (1)
Pubmed 8 references available
Quantity 100 µg
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Catalog No. ABIN361716
382.80 $
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Immunogen Recombinant human Hsp90alpha Specificity mapped to AA 291-304
Clone Hyb-K41220A
Isotype IgG2a
Specificity Detects 90 kDa proteins corresponding to the molecular mass of hsp90 α or β.
Sensitivity 1 µg/ml was sufficient for detection of Hsp90alphabeta 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
Alternative Name Hsp90 alpha/beta
Background Synonyms:
Hsp86, Hsp89A, Hsp90AA1, Hsp90Alpha, HspC1, HSPCA, HspCAL3, Hsp84, Hsp90B, HspC2, HspCB, D6S182, FLJ26984
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. Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. 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 labelof 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. 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.
Gene ID 3326, 3320
NCBI Accession NP_031381, NP_001017963
UniProt P07900, P08238
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: 1 µg/mL was sufficient for detection of hsp90αβ by Western Blot in 20 µg of HeLa lysate.
Restrictions For Research Use only
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
anti-Heat Shock Protein 90 alpha/beta (HSP90 alpha/beta) (AA 291-304) antibody Hsp90 (K41220A), CellLine copy.
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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