anti-HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361718
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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
Catostomus commersonii, Chicken, Dog (Canine), Fish, Galeorhinus galeus, Human, Mustelus antarcticus (Gummy shark), Rabbit, Rat (Rattus), Shark
(254), (161), (147), (94), (72), (23), (22), (22), (20), (19), (19), (19), (19), (18), (18), (18), (18), (13), (6), (3), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
(190), (102), (7), (1)
Clonality (Clone)
Monoclonal ()
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 17 references available
Quantity 200 μg
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Immunogen Recombinant human HSP90beta
Clone H9010
Specificity Detects 90 kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.
Sensitivity 1 µg/mL of SMC-107 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 antibody.
Purification Protein G Purified
Alternative Name HSP90 (HSP90 Antibody Abstract)
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 it's 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 Cancer, Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2500), IHC (1:200)
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
Western Blotting (WB) image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Hsp90 (H9010) Western Blotting, heat shock Hela.
Image no. 2 for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Hsp90 (H9010), cell lines.
Image no. 3 for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Rabbit reticulocyte lysate
Product cited in: Teigen, Orczewska, McLaughlin et al.: "Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback." in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, Vol. 188, pp. 139-47, 2015 (PubMed).

Jayaprakash, Dong, Zou et al.: "Hsp90α and Hsp90β together operate a hypoxia and nutrient paucity stress-response mechanism during wound healing." in: Journal of cell science, Vol. 128, Issue 8, pp. 1475-80, 2015 (PubMed).

Bessemer, Butler, Tunnah et al.: "Cardiorespiratory toxicity of environmentally relevant zinc oxide nanoparticles in the freshwater fish Catostomus commersonii." in: Nanotoxicology, pp. 1-10, 2014 (PubMed).

Hunter, OHagan, Kenyon et al.: "Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells." in: PLoS ONE, Vol. 9, Issue 1, pp. e86842, 2014 (PubMed).

Patel, Yan, Seidler et al.: "Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2." in: Nature chemical biology, Vol. 9, Issue 11, pp. 677-84, 2013 (PubMed).

Espallergues, Teegarden, Veerakumar et al.: "HDAC6 regulates glucocorticoid receptor signaling in serotonin pathways with critical impact on stress resilience." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 32, Issue 13, pp. 4400-16, 2012 (PubMed).

Chen, Prior, Dargusch et al.: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." in: PLoS ONE, Vol. 6, Issue 12, pp. e27865, 2011 (PubMed).

Taldone, Zatorska, Patel et al.: "Design, synthesis, and evaluation of small molecule Hsp90 probes." in: Bioorganic & medicinal chemistry, Vol. 19, Issue 8, pp. 2603-14, 2011 (PubMed).

Gershburg, Murphy, Marschall et al.: "Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization." in: The Biochemical journal, Vol. 431, Issue 2, pp. 227-35, 2010 (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).

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

Loo, Jensen, Cui et al.: "Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome." in: The EMBO journal, Vol. 17, Issue 23, pp. 6879-87, 1999 (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).

Barent, Nair, Carr et al.: "Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes." in: Molecular endocrinology (Baltimore, Md.), Vol. 12, Issue 3, pp. 342-54, 1998 (PubMed).

Nemoto, Sato, Iwanari et al.: "Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis." in: The Journal of biological chemistry, Vol. 272, Issue 42, pp. 26179-87, 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).

Minami, Kawasaki, Miyata et al.: "Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90." in: The Journal of biological chemistry, Vol. 266, Issue 16, pp. 10099-103, 1991 (PubMed).

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Catalog No. ABIN361718
$ 399.30
Plus shipping costs $45.00
200 μg
$ 399.30

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