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Heat Shock Protein 90 (HSP90) antibody

Details for Product No. ABIN361711
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Antigen
Synonyms
git10, swo1, HSP90, htpG, SCBAC25F8.08, 23.m06066, 17.m07646, HSP90-1, 143198_at, 83, 83K HSP, DMHSP82, E(sev)3A, E(sina)2, HSP82, HSP83, ORF1, Su(Raf)3A, anon-EST:Liang-2.53, anon-WO0068693, anon-WO0 ... show more
git10, swo1, HSP90, htpG, SCBAC25F8.08, 23.m06066, 17.m07646, HSP90-1, 143198_at, 83, 83K HSP, DMHSP82, E(sev)3A, E(sina)2, HSP82, HSP83, ORF1, Su(Raf)3A, anon-EST:Liang-2.53, anon-WO0068693, anon-WO0140519.209, clone 2.53, en(lz)3C/4C, hsp84, l(3)j5C2, ms(3)08445, stc, DmelCG1242, CG1242, 86kDa, 89kDa, AL024080, AL024147, Hsp86-1, Hsp89, Hsp90, Hspca, hsp4, Hsp86, EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, LAP2, hsp86, hsp89, hsp90, hsp90a, hspc1, hspca, hspn, lap2, D6S182, HSP84, HSP90B, HSPC2, HSPCB show less
Reactivity
Human, Rabbit, Rat (Rattus), Chicken, Achlya, Wheat germ, Insect cells (Sf9)
(139), (54), (53), (29), (22), (12), (7), (5), (5), (3), (3), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Host
Mouse
(109), (50), (6), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(5), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1)
Application
Western Blotting (WB), Immunohistochemistry (IHC)
(144), (88), (82), (70), (38), (31), (25), (9), (4), (2), (2)
Pubmed 7 references available
Quantity 50 µg
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Catalog No. ABIN361711
201.30 $
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Immunogen Heat shock protein 900 from the water mold Achyla ambisexualis
Clone AC-16
Isotype IgG2b
Specificity This antibody is reactive with both the constitutive and the inducible form of Hsp90. It does not bind to the native form and does not recognize Hsp90 from E.coli or yeast.
Sensitivity 1 µg/mL of SMC-112 was sufficient for detection of Hsp90 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody
Purification Protein G Purified
Alternative Name Hsp90
Background Synonyms:
Hsp84, Hsp86, Hsp90, Hsp89, Hsp90Beta, Hsp90A, Hsp90AA1, Hsp90AB1, Hsp90B, Hsp90N, HspC1, HspC2, HspCA, HspCAL1, HspCAL4, HspCB, HspN, LAP2
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. 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 todate 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 immuno-adsorption 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
NCBI Accession NP_031381.2
UniProt Q8LLI5
Research Area Cancer, Heat Shock Proteins
Application Notes Recommended Dilution: 1 µg/mL was sufficient for detection of hsp90 by Western Blot in 20 µg of HeLa lysate.
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.4, 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 (HSP90) antibody HO-1 (1F12-A6), recombinant HO-1
anti-Heat Shock Protein 90 (HSP90) antibody (2) Hsp90 (AC-16), Mouse Colon 1 in 2000, Amplifier
anti-Heat Shock Protein 90 (HSP90) antibody (3) Hsp90 (AC-16), Human Colon Cancer 1 in 2000, Amplifier
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).

General 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).

Neckers: "Hsp90 inhibitors as novel cancer chemotherapeutic agents." in: Trends in molecular medicine, Vol. 8, Issue 4 Suppl, pp. S55-61, 2002 (PubMed).

Pratt, Toft: "Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery." in: Experimental biology and medicine (Maywood, N.J.), Vol. 228, Issue 2, pp. 111-33, 2003 (PubMed).

Validation Images
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