HSP73 Recombinant Protein (Bovine) (OPED00063)

Catalog No: OPED00063

Size:200 ug

SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 0.5ug of Recombinant Hsc70 (HSP73) Protein.

Product Info

• Predicted Species Reactivity: Bos taurus|Bovine
• Product Format: Liquid. In 30mM TRIS-HCl, pH 7.5, containing 1.0mM EDTA, 2.0mM DTT, and 300mM sodium chloride.
• Host: E. Coli
• Application: WB
• Additional Information: The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.
• Reconstitution and Storage: Store at -80C
• Purification: Purified by multi-step chromatography.
• Purity: >90% (SDS-PAGE; Western blot)
• Application Info: ATPase activity assay (positive). Western blot control.
• Reference: Selection and identification of ligand peptides targeting a model of castrate-resistant osteogenic prostate cancer and their receptors: J. Mandelin, et al.; PNAS 112, 3776 (2015), Application(s): Western Blotting, Abstract; Full Text
  The cyclopentenone prostaglandin 15-deoxy-delta(12,14)- PGJ2 attenuates the development of colon injury caused by dinitrobenzene sulphonic acid in the rat: C. Thiemermann, et al. ; Br. J. Pharmacol. 138, 678 (2003), Application(s): WB , Abstract;
  Tissue-specific expression of inducible and constitutive Hsp70 isoforms in the western painted turtle: L.T. Buck, et al. ; J. Exp. Biol. 206, 303 (2003), Application(s): WB , Abstract;
  Patterns of variation in levels of hsp70 in natural rocky shore populations from microscales to mesoscales: P.M. Halpin, et al.; Integr. Comp. Biol. 42, 815 (2002), Application(s): WB , Abstract;
  Possible association of non-binding of HSP70 to HLA-DRB1 peptide sequences and protection from rheumatoid arthritis: G.E. Dannecker, et al. ; Immunogenetics 54, 67 (2002), Abstract;
  Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity: A.T. Panganiban, et al. ; Cell Stress Chaperones 7, 258 (2002), Application(s): WB , Abstract;

Target Info

• Gene Symbol: HSPA8
• Gene Full Name: heat shock protein family A (Hsp70) member 8
• Alias Symbols: heat shock 70 kDa protein 8;heat shock 70kd protein 10 (HSC71);heat shock 70kDa protein 8;heat shock cognate 71 kD protein;heat shock cognate 71 kDa protein;Hsc70;Hsc70 ATPase;HSPA10.
• NCBI Gene Id: 281831
• Protein Name: Heat shock cognate 71 kDa protein
• Description of Target: 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.
• Uniprot ID: P19120
• Protein Accession #: NP_002825.3
• Nucleotide Accession #: NM_002834.3
• Protein Size (# AA): Recombinant
• Molecular Weight: 73 kDa