HSPA1A Recombinant Protein
Product Sizes
50 ug
£647.00
OPED00070-50UG
About this Product
- SKU:
- OPED00070
- Additional Names:
- dnaK-type molecular chaperone HSP70-1;epididymis secretory protein Li 103;epididymis secretory sperm binding protein;heat shock 70 kDa protein 1;heat shock 70 kDa protein 1/2;heat shock 70 kDa protein 1A;heat shock 70 kDa protein 1A/1B;Heat shock 70 kDa protein 1B;Heat shock 70 kDa protein 2;heat shock 70kD protein 1A;heat shock 70kD protein 1B;heat shock 70kDa protein 1A;heat shock 70kDa protein 1B;heat shock-induced protein;HEL-S-103;HSP70.1;HSP70.1/HSP70.2;HSP70.2;HSP70-1;HSP70-1/HSP70-2;HSP70-1A;HSP70-1B;HSP70-2;HSP70I;HSP72;HSPA1;HSX70.
- Extra Details:
- 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).|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).
- Gene Details:
- heat shock protein family A (Hsp70) member 1A|heat shock protein family A (Hsp70) member 1B
- Host:
- E. coli
- Molecular Weight:
- 72 kDa
- Protein Details:
- Heat shock 70 kDa protein 1A|Heat shock 70 kDa protein 1B
- Purity:
- >95% (SDS-PAGE; Western blot)
- Purification:
- Purified by multi-step chromatography.
- Shipping Conditions:
- Dry Ice
- Storage Conditions:
- Store at -80C
- Supplier:
- Aviva Systems Biology
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
- Manufacturer's Data Sheet:html_datasheet.php
