HSPA8 Antibody
Product Sizes
50 ug
£431.00
OAED00187-50UG
About this Product
- SKU:
- OAED00187
- Additional Names:
- constitutive heat shock protein 70;dnaK-type molecular chaperone HSP70-1;epididymis luminal protein 33;epididymis secretory protein Li 103;epididymis secretory sperm binding protein;epididymis secretory sperm binding protein Li 72p;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 70 kDa protein 8;heat shock 70kd protein 10;heat shock 70kD protein 1A;heat shock 70kD protein 1B;heat shock 70kDa protein 1A;heat shock 70kDa protein 1B;heat shock 70kDa protein 8;heat shock cognate 71 kDa protein;heat shock cognate protein 54;heat shock-induced protein;HEL-33;HEL-S-103;HEL-S-72p;HSC54;HSC70;HSC71;HSP70.1;HSP70.1/HSP70.2;HSP70.2;HSP70-1;HSP70-1/HSP70-2;HSP70-1A;HSP70-1B;HSP70-2;HSP70I;HSP71;HSP72;HSP73;HSPA1;HSPA10;HSX70;LAP1;LAP-1;lipopolysaccharide-associated protein 1;LPS-associated protein 1;NIP71;N-myristoyltransferase inhibitor protein 71.
- translate.label.attr.clone:
- N27F34
- Clonality:
- Monoclonal
- Conjugate:
- R-PE
- 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 (PubMed:21150129; PubMed:21148293; PubMed:24732912; PubMed:27916661; PubMed:23018488). This is achieved through cycles of ATP binding; ATP hydrolysis and ADP release; mediated by co-chaperones (PubMed:21150129; PubMed:21148293; PubMed:24732912; PubMed:27916661; PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70; but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129; PubMed:21148293; PubMed:24732912; PubMed:27916661; PubMed:23018488). The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange; which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones 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:24318877; PubMed:27474739; PubMed:24121476; PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response; including TNF secretion by monocytes (PubMed:10722728; PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).|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|heat shock protein family A (Hsp70) member 8
- Host:
- Mouse
- Immunogen:
- Native human Hsp70/Hsc70.
- Isotype:
- IgG1
- Protein Details:
- Heat shock 70 kDa protein 1A|Heat shock cognate 71 kDa protein
- Purity:
- Protein G affinity purified.<br/>
- Shipping Conditions:
- Blue Ice
- Storage Conditions:
- Long Term Storage : +4C
- Supplier:
- Aviva Systems Biology
- Type:
- Antibodies: Monoclonal Antibody
- Manufacturer's Data Sheet:html_datasheet.php
