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. The protein coding region of the substrate binding domain of DNAK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid(Met) is attached at N- terminus
Size
0.5mg, 100ug, 20ug
Concentration
n/a
Applications
SDS-PAGE
Other Names
Dnak (C-term, 385-638), Substrate binding domain, Heat shock protein 70, Heat shock 70 kDa protein, HSP70, Chaperone protein dnaK, Chaperone Hsp 70, Co chaperone with DnaJ, dnaK, Heat shock 70 kDa protein,