HSPA1A Recombinant Protein (Human) (OPED00070)

Catalog No: OPED00070

Size:50 ug

SDS-PAGE analysis: Lane 1: MW marker; Lane 2: 0.5ug; Lane 3: 1ug; Lane 4: 2ug; Lane 5: 5ug Hsp70

Product Info

• Predicted Species Reactivity: Homo sapiens|Human
• Product Format: Liquid. In Dulbecco's PBS.
• Host: E. Coli
• Application: ELISA, IHC, WB
• Additional Information: The Hsp70 family of heat shock protiens 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: >95% (SDS-PAGE; Western blot)
• Application Info: ATPase activity assay (positive). Western blot control.
• Reference: Growth and repair factors, osteoactivin, matrix metalloproteinase and heat shock protein 72, increase with resolution of inflammation in musculotendinous tissues in a rat model of repetitive grasping: N. Frara, et al.; BMC Musculoskelet. Dis. 17, 34 (2016), Application(s): Western blot, Abstract; Full Text
  Identification of low-abundance proteins in serum via the isolation of HSP72 complexes: M. Tanaka, et al.; J. Proteomics (2016), Application(s): Heat shock, Abstract;
  CpG-A stimulates Hsp72 secretion from plasmacytoid dendritic cells, facilitating cross-presentation: T. Tanaka, et al.; Immunol. Lett. 167, 34 (2015), Application(s): ELISAusing human or murine DCs , Abstract;
  UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP: Y. Teng, et al.; Biochem. Pharmacol. 97, 518 (2015), Application(s): Heat shock, Abstract;
  Quantitative Analysis of Liposomal Heat Shock Protein 70 (Hsp70) in the Blood of Tumor Patients Using a Novel LipHsp70 ELISA: S. Breuninger, et al.; J. Clin. Cell. Immunol. 5, 1 (2014), Application(s): Cell Culture, Western Blotting, Full Text
  Antigen microarrays identify unique serum autoantibody signatures in clinical and pathologic subtypes of multiple sclerosis: H. Weiner, et al. ; PNAS 105, 18889 (2008), Application(s): Antigen Microarray using human serum, Abstract;
  Antigen microarrays identify unique serum autoantibody signatures in clinical and pathologic subtypes of multiple sclerosis: F.J. Quintana, et al.; PNAS 105, 18889 (2008), Abstract;
  Complex Formation between Heat Shock Protein 72 and Hepatitis B VirusX Protein in Hepatocellular Carcinoma Tissues: X. Wang, et al. ; J. Proteome Res. 7, 5133 (2008), Application(s): IHC using human tissue, Abstract;
  Extracellular HSP70 blocks CD40L-induced apoptosis and tubular formation in endothelial cells: S. Futagami, et al. ; J. Gastroenterol. Hepatol. 23, S222 (2008), Application(s): Apoptosis Assay using human samples, Abstract;
  Increased serum levels of heat shock protein 70 are associated with low risk of coronary artery disease: J. Zhu, et al.; Arterioscler. Thromb. Vasc. Biol. 23, 1055 (2003), Abstract;
  Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein: M. Oglesbee, et al. ; J. Virol. 76, 8737 (2002), Application(s): Micro Array using human samples, Abstract;
  Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein: X. Zhang, et al.; J. Virol. 76, 8737 (2002), Abstract;
  Microglial activation and amyloid-beta clearance induced by exogenous heat-shock proteins: S. Shimohama, et al. ; FASEB J. 16, 601 (2002), Application(s): In Vitro Assay using human samples, Abstract;
  Microglial activation and amyloid-beta clearance induced by exogenous heat-shock proteins: J. Kakimura, et al.; FASEB J. 16, 601 (2002), Abstract;
  The anti-apoptotic function of hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC: G.C. Bagby, et al. ; J. Biol. Chem. 277, 49638 (2002), Application(s): Other using human samples, Abstract;
  The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation: V.L. Cryns, et al. ; J. Biol. Chem. 276, 16059 (2001), Application(s): In Vitro Assay using human samples, Abstract;
  The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome: J. Luders, et al.; J. Biol. Chem. 275, 4613 (2000), Abstract; Full Text
  Chaperone-mediated protein folding: A.L. Fink; Physiol. Rev. 79, 425 (1999), Abstract;
  Two distinct domains in hsc70 are essential for the interaction with the synaptic vesicle cysteine string protein: B. Stahl, et al.; Eur. J. Cell Biol. 78, 375 (1999), Abstract;
  A hitchhiker's guide to the human Hsp70 family: M. Tavaria, et al.; Cell Stress Chaperones 1, 23 (1996), Abstract;

Target Info

• Gene Symbol: HSPA1A|HSPA1B
• Gene Full Name: heat shock protein family A (Hsp70) member 1A|heat shock protein family A (Hsp70) member 1B
• Alias Symbols: 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.
• NCBI Gene Id: 3303|3304
• Protein Name: Heat shock 70 kDa protein 1A|Heat shock 70 kDa protein 1B
• 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, 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).
• Uniprot ID: P0DMV8|P0DMV9
• Protein Accession #: NP_001057.1
• Nucleotide Accession #: NM_001066.2
• Protein Size (# AA): Recombinant
• Molecular Weight: 72 kDa