Volume : 50 µg
Clone Number :
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
Product Type : polyclonal Ab Antibody
Immunogen Species : Homo sapiens (Human)
UniProt ID : P0DMV8
Immunogen : Recombinant Human Heat shock 70 kDa protein 1A protein (418-512AA)
Raised in : Rabbit
Species Reactivity : Human
Tested Applications :
Background : Molec µLar chaperone implicated in a wide variety of cell µLar processes, including protection of the proteome from stress, folding and transport of newly syntheVolumed 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 thro µgh cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only reg µLate 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 reg µLated 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 thro µgh 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 (stim µLate 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 cell µLar stress thro µgh 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). Reg µLates 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 reg µLatory T-cells (Treg) during inflammation (PubMed : 23973223). Negatively reg µLates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed : 9499401).
Clonality : polyclonal Ab
Isotype : IgG
Purification Method : >95%, Protein G purified
Conj µgate : FITC
Buffer : Preservative : 0.03% Proclin 300
Constituents : 50% Glycerol, 0.01M PBS, pH 7.4
Form : Liquid
Stroage : Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Target Names : HSPA1A
Research Areas : Others
