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Recombinant E.coli DnaK Chaperone Hsp70, Co-chaperone with DnaJ (1-384)

Cat.No.
DnaK-314E
Species
E. coli
Product Name
Recombinant E.coli DnaK Chaperone Hsp70, Co-chaperone with DnaJ (1-384)
Product Overview
The ATPase domain of recombinant DNAK was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques (384 aa, 41.6 kDa).
Description
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain(residues385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector.
Source
E. coli
Form
Liquid. In 25 mM Tris-HCl buffer (pH 7.5) containing 100 mM NaCl, 5 mM DTT, 10% glycerol.
Purity
> 95% by SDS – PAGE.
Storage
Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.
Concentration
1 mg/ml (determined by Bradford assay).
Gene Name
Synonyms
dnaK; dnaK chaperone Hsp70, co-chaperone with DnaJ; Hsp70 protein; ECK0014; groPAB; groPC; groPF; grpC; grpF; JW0013; seg; chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins.
Gene ID
Protein Refseq
UniProt ID
P0A6Y8
Data Sheet
MSDS
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