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DnaK (E. coli), (recombinant)

ADI-SPP-630

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ADI-SPP-630-J — 1 mg

$1,801.00

DnaK (E. coli), (recombinant) quantity
ADI-SPP-630-D — 50 µg

$262.00

DnaK (E. coli), (recombinant) quantity
ADI-SPP-630-F — 200 µg

$620.00

DnaK (E. coli), (recombinant) quantity

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.

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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.

Product Details

Alternative Name	Heat shock protein 70, HSP70
Application Notes	ATPase activity assay (positive). Western blot control.
Formulation	Liquid. In 40mM TRIS, pH 7.5, containing 80mM sodium chloride, 0.8mM DTT, 0.08mM PMSF, and 20% glycerol.
MW	~70kDa
Purity	≥95% (SDS-PAGE; Western blot)
Purity Detail	Purified by multi-step chromatography.
Source	Produced in E. coli.
UniProt ID	P0A6Y8 (strain K12)

Handling & Storage

Long Term Storage	-80°C
Shipping	Dry Ice

Regulatory Status	RUO – Research Use Only

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
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
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

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DnaK (E. coli), (recombinant)

ADI-SPP-630

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

Manuals And Inserts

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