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DnaK (E. coli), (recombinant)

ADI-SPP-630-D 50 µg 255.00 USD
ADI-SPP-630-F 200 µg 602.00 USD
ADI-SPP-630-J 1 mg 1,749.00 USD
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Product Details

Alternative Name:Heat shock protein 70, HSP70
Source:Produced in E. coli.
UniProt ID:P0A6Y8 (strain K12)
Formulation:Liquid. In 40mM TRIS, pH 7.5, containing 80mM sodium chloride, 0.8mM DTT, 0.08mM PMSF, and 20% glycerol.
Purity:≥95% (SDS-PAGE; Western blot)
Purity Detail:Purified by multi-step chromatography.
Applications:ELISA, WB
Activity assay, in vitro Assay
Application Notes:ATPase activity assay (positive). Western blot control.
Shipping:Dry Ice
Long Term Storage:-80°C
Scientific Background:DnaK possesses an autophosphorylation activity and a weak 5-nucleotidase activity, cleaving the 5 phosphate groups from both ribose and deoxyribose nucleotides. The role of DnaK in ATP-dependent protein-protein interactions has been extended to normal E. coli physiology, where, like eukaryotic Hsp70 homologs, it is thought to participate in the assembly/disassembly of protein complexes.
Regulatory Status:RUO - Research Use Only
DnaK (E. coli), (recombinant) SDS-PAGE
SDS-PAGE analysis of DnaK: Lane 1: MWM, Lanes 2-5: 0.5, 1, 2, 5µg of Prod. No. ADI-SPP-630.
DnaK (E. coli), (recombinant) Western blot
Western Blot Analysis of DnaK: Lane 1: MWM, Lanes 2: 100ng of Prod. No. ADI-SPP-630; probed with Prod. No. ADI-SPA-880.
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DnaK (E. coli), (recombinant) SDS-PAGE DnaK (E. coli), (recombinant) Western blot

Product Literature References

GmDNJ1, a type-I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean: K.P. Li, et al.; Plant Direct 5, e00298 (2021), Abstract; Full Text
Protein polarization driven by nucleoid exclusion of DnaK(HSP70)-substrate complexes: C. Collet, et al.; Nat. Commun. 9, 2027 (2018), Abstract; Full Text
Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes: V. Lopez, et al.; Cell Stress Chaperones 21, 609 (2016), Abstract; Full Text
Scope and limitations of the designer proline-rich antibacterial peptide dimer, A3-APO, alone or in synergy with conventional antibiotics: J.r. Otvos, et al. ; Peptides 29, 1878 (2008), Application(s): WB , Abstract;
Monitoring of the heat-shock response in Escherichia coli using an optical biosensor: C.F. Mandenius, et al. ; Anal. Biochem. 322, 156 (2003), Application(s): EIA , Abstract;
Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity: M. Zolkiewski, et al. ; J. Mol. Biol. 321, 111 (2002), Abstract;
NEMO trimerizes through its coiled-coil C-terminal domain: M. Veron, et al. ; J. Biol. Chem. 277, 17464 (2002), Application(s): In Vitro Assay , 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;
The conserved helix C region in the superfamily of interferon-gamma /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK: B. Walker, et al. ; J. Biol. Chem. 277, 25668 (2002), Abstract;

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