HSP70 1A Antikörper (AA 418-512)

Produktnummer ABIN7154867

Produktdetails anti-HSP70 1A Antikörper

Target: HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

Bindungsspezifität: AA 418-512

Reaktivität: Human

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser HSP70 1A Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF)

Kreuzreaktivität: Human

Aufreinigung: >95%, Protein G purified

Immunogen: Recombinant Human Heat shock 70 kDa protein 1A protein (418-512AA)

Isotyp: IgG

Anwendungsinformationen

Applikationshinweise: Recommended dilution: WB:1:500-1:5000, IHC:1:200-1:500, IF:1:50-1:200,

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

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.

Details zu HSP70 1A

Target: HSP70 1A (HSPA1A) (Heat Shock 70kDa Protein 1A (HSPA1A))

Andere Bezeichnung: HSPA1A (HSPA1A Produkte)

Synonyme: hsp70-4 antikoerper, hspa1a antikoerper, Hsp70-3 antikoerper, Hsp70.3 antikoerper, Hsp72 antikoerper, hsp68 antikoerper, hsp70A1 antikoerper, HSP72 antikoerper, Hsp70-1 antikoerper, Hspa1 antikoerper, Hspa1b antikoerper, hsp70-1 antikoerper, hsp70-1a antikoerper, hsp70i antikoerper, hsp72 antikoerper, hspa1 antikoerper, hspa1b antikoerper, HSP70-1 antikoerper, HSP70-1A antikoerper, HSP70I antikoerper, HSPA1 antikoerper, HSPA1A antikoerper, HSPA1B antikoerper, HSP70-2 antikoerper, HSPA2 antikoerper, HSP70 antikoerper, hspA1A antikoerper, heat shock cognate 70-kd protein, tandem duplicate 3 antikoerper, heat shock 70 kDa protein 1 antikoerper, heat shock 70 kDa protein II antikoerper, heat shock protein 1A antikoerper, heat shock 70kD protein 1A antikoerper, heat shock protein family A (Hsp70) member 1A S homeolog antikoerper, heat shock protein family A (Hsp70) member 1A antikoerper, heat shock protein 70.2 antikoerper, heat shock 70kDa protein 1A antikoerper, heat shock 70 kDa protein 1B antikoerper, heat shock protein 70.1 antikoerper, hsp70.3 antikoerper, LOC100023597 antikoerper, LOC100554002 antikoerper, LOC100608888 antikoerper, Hspa1a antikoerper, hspa1a.S antikoerper, HSPA1A antikoerper, HSP70.2 antikoerper, LOC100354037 antikoerper, HSP70.1 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). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).

Aliases: HSPA1A antibody, HSP72 antibody, HSPA1 antibody, HSX70Heat shock 70 kDa protein 1A antibody, Heat shock 70 kDa protein 1 antibody, HSP70-1 antibody, HSP70.1 antibody

UniProt: P0DMV8

Pathways: Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process