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HSP90AA2 Antikörper

HSP90AA2 Reaktivität: Human WB, ELISA, IHC, IP, IF, ICC Wirt: Maus Monoclonal 2G5-G3 unconjugated
Produktnummer ABIN361663
  • Target Alle HSP90AA2 Antikörper anzeigen
    HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))
    Reaktivität
    • 76
    • 51
    • 19
    • 4
    • 3
    • 3
    • 3
    • 3
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human
    Wirt
    • 44
    • 30
    • 2
    • 1
    Maus
    Klonalität
    • 39
    • 38
    Monoklonal
    Konjugat
    • 22
    • 5
    • 4
    • 4
    • 3
    • 3
    • 3
    • 3
    • 3
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    Dieser HSP90AA2 Antikörper ist unkonjugiert
    Applikation
    • 69
    • 34
    • 27
    • 26
    • 22
    • 14
    • 14
    • 13
    • 10
    • 6
    • 2
    • 1
    • 1
    • 1
    • 1
    Western Blotting (WB), ELISA, Immunohistochemistry (IHC), Immunoprecipitation (IP), Immunofluorescence (IF), Immunocytochemistry (ICC)
    Spezifität
    Detects ~90 kDa. HSP90α-specific (>96 % α-specific by ELISA)
    Kreuzreaktivität
    Human, Maus, Ratte
    Aufreinigung
    Protein G Purified
    Immunogen
    Recombinant Full Length Human HSP90alpha Protein
    Klon
    2G5-G3
    Isotyp
    IgG1
  • Applikationshinweise
    • WB (1:2000)
    • ICC/IF (1:100)
    • optimal dilutions for assays should be determined by the user.
    Kommentare

    0.5 μg/ml of ABIN361663 was sufficient for detection of HSP90alpha in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Konzentration
    1 mg/mL
    Buffer
    PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
    Konservierungsmittel
    Sodium azide
    Vorsichtsmaßnahmen
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Lagerung
    -20 °C
    Informationen zur Lagerung
    -20°C
  • Ortega, Calvillo, Luna, Pérez-Severiano, Rubio-Osornio, Guevara, Limón: "17-AAG improves cognitive process and increases heat shock protein response in a model lesion with A?25-35." in: Neuropeptides, Vol. 48, Issue 4, pp. 221-32, (2014) (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).

  • Target
    HSP90AA2 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2 (HSP90AA2))
    Andere Bezeichnung
    HSP90 alpha (HSP90AA2 Produkte)
    Synonyme
    HSP90ALPHA antikoerper, HSPCA antikoerper, HSPCAL3 antikoerper, heat shock protein 90 alpha family class A member 2, pseudogene antikoerper, HSP90AA2P antikoerper
    Hintergrund
    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 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 (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.
    Gen-ID
    3320
    NCBI Accession
    NP_001017963
    UniProt
    P07900
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