HSP90 anticorps

N° du produit ABIN361718

Cet anticorps Souris Monoclonal détecte spécifiquement HSP90 dans WB, IP, IHC, ELISA, IF, ICC et AA. Il présente une réactivité envers Humain et a été mentionné dans 11+ publications.

Aperçu rapide pour HSP90 anticorps (ABIN361718)

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

Reactivité: Humain

Hôte: Souris

Clonalité: Monoclonal

Conjugué: Cet anticorp HSP90 est non-conjugé

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

Clone: H9010

Détail du produit anti-HSP90 anticorps

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

Réactivité croisée: Poulet, Chien, Poisson, Hamster, Humain, Souris, Lapin, Rat, Requin

Purification: Protein G Purified

Immunogène: Recombinant human HSP90beta

Isotype: IgG2a

Information d'application

Indications d'application:

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

Commentaires:

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

Stockage

Format: Liquid

Concentration: 1 mg/mL

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

Agent conservateur: Sodium azide

Précaution d'utilisation: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Stock: -20 °C

Stockage commentaire: -20°C

Références pour anticorps anti-HSP90 (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." dans: 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. ..." dans: 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." dans: 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." dans: 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." dans: 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." dans: 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." dans: 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." dans: 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." dans: 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." dans: 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." dans: The Biochemical journal, Vol. 431, Issue 2, pp. 227-35, (2010) (PubMed).

Détails sur HSP90

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

Autre désignation: HSP90

Sujet: 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.

ID gène: 3326

NCBI Accession: NP_031381

UniProt: P08238

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