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HSPA1B Antikörper (AA 418-641) (HRP)

HSPA1B Reaktivität: Human ELISA Wirt: Kaninchen Polyclonal HRP
Produktnummer ABIN7154874
  • Target Alle HSPA1B Antikörper anzeigen
    HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))
    Bindungsspezifität
    • 6
    • 3
    • 2
    • 2
    • 1
    • 1
    • 1
    AA 418-641
    Reaktivität
    • 11
    • 8
    • 6
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human
    Wirt
    • 19
    • 3
    Kaninchen
    Klonalität
    • 20
    • 2
    Polyklonal
    Konjugat
    • 10
    • 6
    • 5
    • 1
    Dieser HSPA1B Antikörper ist konjugiert mit HRP
    Applikation
    • 16
    • 11
    • 9
    • 6
    • 5
    • 2
    • 2
    • 2
    • 1
    ELISA
    Kreuzreaktivität
    Human
    Aufreinigung
    >95%, Protein G purified
    Immunogen
    Recombinant Human Heat shock 70 kDa protein 1B protein (418-641AA)
    Isotyp
    IgG
    Top Product
    Discover our top product HSPA1B Primärantikörper
  • Applikationshinweise
    Optimal working dilution should be determined by the investigator.
    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Buffer
    Preservative: 0.03 % Proclin 300
    Constituents: 50 % Glycerol, 0.01M PBS, pH 7.4
    Konservierungsmittel
    ProClin
    Vorsichtsmaßnahmen
    This product contains ProClin: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Lagerung
    -20 °C,-80 °C
    Informationen zur Lagerung
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • Target
    HSPA1B (Heat Shock 70kDa Protein 1B (HSPA1B))
    Andere Bezeichnung
    HSPA1B (HSPA1B Produkte)
    Synonyme
    HSP70-1B antikoerper, HSP70-2 antikoerper, APG-2 antikoerper, HS24/P52 antikoerper, HSPH2 antikoerper, RY antikoerper, hsp70 antikoerper, hsp70RY antikoerper, ARABIDOPSIS THALIANA HEAT SHOCK COGNATE PROTEIN 70-1 antikoerper, AT-HSC70-1 antikoerper, HEAT SHOCK COGNATE PROTEIN 70 antikoerper, HEAT SHOCK PROTEIN 70-1 antikoerper, HSC70 antikoerper, HSP70-1 antikoerper, T22P11.90 antikoerper, T22P11_90 antikoerper, heat shock cognate protein 70-1 antikoerper, Hsp70 antikoerper, Hsp70-1 antikoerper, Hsp70.1 antikoerper, hsp68 antikoerper, HSPA1A antikoerper, HSPA1B antikoerper, HSPA2 antikoerper, HSP70.2 antikoerper, Hsp70-2 antikoerper, Hsp72 antikoerper, Hspa1 antikoerper, Hspa1a antikoerper, Hspa2 antikoerper, heat shock protein family A (Hsp70) member 1B antikoerper, heat shock protein family A (Hsp70) member 4 antikoerper, heat shock cognate protein 70-1 antikoerper, heat shock protein 1B antikoerper, heat shock protein 70.2 antikoerper, heat shock 70kDa protein 1A antikoerper, heat shock 70kD protein 1B (mapped) antikoerper, HSPA1B antikoerper, HSPA4 antikoerper, HSC70-1 antikoerper, Hspa1b antikoerper, HSP70.2 antikoerper, HSPA1A antikoerper
    Hintergrund

    Background: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).

    Aliases: HSPA1B antibody, HSP72 antibody, Heat shock 70 kDa protein 1B antibody, Heat shock 70 kDa protein 2 antibody, HSP70-2 antibody, HSP70.2 antibody

    UniProt
    P0DMV9
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