anti-HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361822
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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
Human, Mouse (Murine), Rat (Rattus)
(254), (161), (146), (95), (73), (24), (22), (22), (20), (20), (19), (19), (19), (19), (19), (19), (19), (13), (6), (3), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
(191), (101), (7), (1)
This HSP90 antibody is un-conjugated
(12), (11), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (9), (8), (2), (2)
ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blotting (WB)
(262), (175), (173), (154), (129), (120), (24), (10), (2), (2)
Pubmed 10 references available
Quantity 25 μL
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Full length protein HSP90
Specificity Detects ~90 kDa.
Purification Rabbit antiserum
Alternative Name HSP90 (HSP90 Antibody Abstract)
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).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Research Area Cancer, Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:40000), ICC/IF (1:100)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Storage -20 °C
Supplier Images
Image no. 1 for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361822) Hsp90, Mouse backskin
Product cited in: Zhang, Pruitt, Tran et al.: "B cell-specific deficiencies in mTOR limit humoral immune responses." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 191, Issue 4, pp. 1692-703, 2013 (PubMed).

Verheyen, Peeraer, Nuydens et al.: "Systemic anti-vascular endothelial growth factor therapies induce a painful sensory neuropathy." in: Brain : a journal of neurology, Vol. 135, Issue Pt 9, pp. 2629-41, 2012 (PubMed).

Wagatsuma, Shiozuka, Kotake et al.: "Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells." in: Molecular and cellular biochemistry, Vol. 358, Issue 1-2, pp. 265-80, 2011 (PubMed).

Background publications 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).

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).

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

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. ABIN361822
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