HSPA8 Recombinant Protein
Product Sizes
10ug
£257.00
OPCD04026-10UG
50ug
£489.00
OPCD04026-50UG
200ug
£875.00
OPCD04026-200UG
About this Product
- SKU:
- OPCD04026
- Additional Names:
- 2410008N15Rik;heat shock 70 kDa protein 8;heat shock cognate 71 kDa protein;heat shock cognate hsc73;heat shock protein cognate 70;Hsc7;Hsc70;Hsc71;Hsc73;Hsp;Hsp73;Hspa10.
- Conjugate:
- Unconjugated
- Concentration:
- 200 ug/mL (prior to lyoph)
- 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 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. 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. 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. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1.
- Gene Details:
- heat shock protein 8
- Host:
- E. coli
- Molecular Weight:
- 11kDa
- Protein Details:
- Heat shock cognate 71 kDa protein
- Purity:
- > 95%
- Shipping Conditions:
- Blue Ice
- Source:
- E.coli
- Storage Conditions:
- 2Â[o]C to 8Â[o]C|-80Â[o]C
- Supplier:
- Aviva Systems Biology
- Type:
- Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
- Manufacturer's Data Sheet:html_datasheet.php
