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HSP70/HSP72 (human), (recombinant)

A molecular chaperone that assists in the folding of emerging polypeptides and the refolding of denatured proteins.
 
ADI-NSP-555-D 50 µg 298.00 USD
 
ADI-NSP-555-F 200 µg 853.00 USD
Do you need bulk/larger quantities?
 

Product Specification

Alternative Name:Heat shock protein 70, HspA1A, HspA1B
 
MW:~72kDa
 
Source:Produced in E. coli.
 
UniProt ID:P0DMV8 (HSPA1A), P0DMV9 (HSPA1B)
 
GenBank ID:M11717
 
Gene/Protein Identifier:NP_005336.3 (RefSeq), NM_005345 (RefSeq), 3303 (Entrez GeneID), 140550 (OMIM)
 
Formulation:Liquid. In Dulbecco's PBS.
 
Purity:≥95% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Endotoxin Content:>500EU/mg purified protein (LAL test)
 
Applications:ELISA, IHC, WB
Activity assay, Antigen microarray, Apoptosis assay, in vitro Assay
 
Application Notes:ATPase activity assay (positive). Western blot control.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background: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.
 
NSP-555 SDS-PAGE
SDS-PAGE analysis: Lane 1: MW marker; Lane 2: 0.5µg; Lane 3: 1µg; Lane 4: 2µg; Lane 5: 5µg Hsp70
NSP-555 WB
Western Blot analysis of HSP70/HSP72 (human), (recombinant): Lane 1: MWM, Lane 2:50 ng HSP70; Lane 3: 50 ng DnaK (Prod. No. ADI-SPP-630) , probed with anti-HSP70 (Prod. No. ADI-SPA-810).
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NSP-555 SDS-PAGE NSP-555 WB

Product Literature References

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 136, 214 (2016), Application(s): Heat shock, Abstract;
Retinoic acid induces nuclear FAK translocation and reduces breast cancer cell adhesion through Moesin, FAK, and Paxillin: A.M. Sanchez, et al.; Mol. Cell. Endocrinol. 430, 1 (2016), Application(s): Immunoblotting, Abstract;
CpG-A stimulates Hsp72 secretion from plasmacytoid dendritic cells, facilitating cross-presentation: T. Tanaka, et al.; Immunol. Lett. 167, 34 (2015), Application(s): ELISA using 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;

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