HSP70 1A anticorps (AA 418-512)

N° du produit ABIN7154867

Cet anticorps Lapin Polyclonal détecte spécifiquement HSP70 1A dans WB, IHC, ELISA et IF. Il présente une réactivité envers Humain.

Aperçu rapide pour HSP70 1A anticorps (AA 418-512) (ABIN7154867)

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

Reactivité: Humain

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp HSP70 1A est non-conjugé

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

Détail du produit anti-HSP70 1A anticorps

Épitope: AA 418-512

Fonction: HSPA1A Antibody

Purification: Protein G purified

Pureté: >95 %

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

Isotype: IgG

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Stockage

Format: Liquid

Buffer: Preservative: 0.03 % Proclin 300
Constituents: 50 % Glycerol, 0.01M PBS, pH 7.4

Agent conservateur: ProClin

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

Stock: -20 °C,-80 °C

Stockage commentaire: Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Détails sur HSP70 1A

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

Autre désignation: HSPA1A

Sujet:

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