Purity: > 95% by SDS - PAGE Format: Liquid. 25 mM Tris-HCl, pH7.5, 100 mM NaCl, 5 mM DTT, 10%Glycerol. . DnaK, originally identified for its DNA replication by bacteriophage lambda 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. The ATPase domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.
Size
0.5mg, 100ug, 20ug
Concentration
n/a
Applications
SDS-PAGE
Other Names
dnaK, Dnak (N-term, 1-384), ATPase binding domain, Heat shock protein 70, Heat shock 70 kDa protein, HSP70, Chaperone protein dnaK, Chaperone Hsp70, Co chaperone with DnaJ,