HSP90 antibody

Catalog No. ABIN361718

Product Details anti-HSP90 Antibody

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90 antibody is un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC), Antibody Array (AA)

Specificity: Detects 90 kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.

Cross-Reactivity: Chicken, Dog, Fish, Hamster, Human, Mouse, Rabbit, Rat, Shark

Purification: Protein G Purified

Immunogen: Recombinant human HSP90beta

Clone: H9010

Isotype: IgG2a

Application Details

Application Notes:

• WB (1:2500)
• IHC (1:100)
• optimal dilutions for assays should be determined by the user.

Comment:

1 μg/ml of ABIN361717 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.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

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

Storage Comment: -20°C

References for anti-HSP90 antibody (ABIN361718)

de la Mare, Jurgens, Edkins: "Extracellular Hsp90 and TGFβ regulate adhesion, migration and anchorage independent growth in a paired colon cancer cell line model." in: BMC cancer, Vol. 17, Issue 1, pp. 202, (2018) (PubMed).

Rodina, Wang, Yan, Gomes, Dunphy, Pillarsetty, Koren, Gerecitano, Taldone, Zong, Caldas-Lopes, Alpaugh, Corben, Riolo, Beattie, Pressl, Peter, Xu, Trondl, Patel, Shimizu, Bolaender, Yang, Panchal et al.: "The epichaperome is an integrated chaperome network that facilitates tumour survival. ..." in: Nature, Vol. 538, Issue 7625, pp. 397-401, (2017) (PubMed).

Jayaprakash, Dong, Zou, Bhatia, OBrien, Chen, Woodley, Li: "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).

Teigen, Orczewska, McLaughlin, OBrien: "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).

Hunter, OHagan, Kenyon, Dhanani, Prinsloo, Edkins: "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).

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

Patel, Yan, Seidler, Patel, Sun, Yang, Que, Taldone, Finotti, Stephani, Gewirth, Chiosis: "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, Boulden, Challis, Jochems, Chan, Petersen, Deneris, Matthias, Hahn, Lucki, Beck, Berton: "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).

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

Chen, Prior, Dargusch, Roberts, Riek, Eichmann, Chiruta, Akaishi, Abe, Maher, Schubert: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." in: PLoS ONE, Vol. 6, Issue 12, pp. e27865, (2011) (PubMed).

Gershburg, Murphy, Marschall, Gershburg: "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).

Target Details for HSP90

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Alternative Name: HSP90 (HSP90 Products)

Synonyms: EL52 antibody, HSP86 antibody, HSP89A antibody, HSP90A antibody, HSP90N antibody, HSPC1 antibody, HSPCA antibody, HSPCAL1 antibody, HSPCAL4 antibody, HSPN antibody, Hsp89 antibody, Hsp90 antibody, LAP2 antibody, git10 antibody, swo1 antibody, HSP90 antibody, htpG antibody, SCBAC25F8.08 antibody, 23.m06066 antibody, 17.m07646 antibody, HSP90-1 antibody, 143198_at antibody, 83 antibody, 83K HSP antibody, DMHSP82 antibody, E(sev)3A antibody, E(sina)2 antibody, HSP82 antibody, HSP83 antibody, ORF1 antibody, Su(Raf)3A antibody, anon-EST:Liang-2.53 antibody, anon-WO0068693 antibody, anon-WO0140519.209 antibody, clone 2.53 antibody, en(lz)3C/4C antibody, hsp84 antibody, l(3)j5C2 antibody, ms(3)08445 antibody, stc antibody, DmelCG1242 antibody, CG1242 antibody, Hsp86 antibody, Hspca antibody, 86kDa antibody, 89kDa antibody, AL024080 antibody, AL024147 antibody, Hsp86-1 antibody, hsp4 antibody, hsp86 antibody, hsp89 antibody, hsp90 antibody, hsp90a antibody, hspc1 antibody, hspca antibody, hspn antibody, lap2 antibody, Hsp90alpha antibody, heat shock protein 90 alpha family class A member 1 antibody, heat shock protein Hsp90 antibody, Hsp90 chaperone antibody, Heat shock protein 90 antibody, heat shock protein 90 antibody, chaperone protein HtpG antibody, molecular chaperone HtpG antibody, Heat Shock Protein 90 antibody, uncharacterized LOC100384473 antibody, Heat shock protein 83 antibody, heat shock protein 90, alpha (cytosolic), class A member 1 antibody, heat shock protein 90 alpha family class B member 1 antibody, heat shock protein 90kDa alpha family class A member 1 L homeolog antibody, heat shock protein HSP 90-alpha antibody, HSP90AA1 antibody, hsp90 antibody, HSP90 antibody, daf-21 antibody, htpG antibody, SCO7516 antibody, MAP_RS10510 antibody, TP04_0646 antibody, TP01_0934 antibody, APH_RS03525 antibody, GbCGDNIH1_0315 antibody, MAV_2118 antibody, HSP90C antibody, BBOV_IV008400 antibody, BBOV_III007380 antibody, ACICU_00312 antibody, ECL_01244 antibody, YE105_C1172 antibody, pco153543(105) antibody, Hsp83 antibody, Hsp90aa1 antibody, HSP90AB1 antibody, hsp90aa1.1.L antibody, LOC108698781 antibody

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). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Gene ID: 3326

NCBI Accession: NP_031381

UniProt: P08238

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals