Purity: > 95% by SDS - PAGE Format: Liquid. In 25 mM Tris-HCl buffer (pH 7.5) containing 100 mM NaCl, 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(residues 508-638) of the substrate binding domain is alpha-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was overexpressed in E. coli and 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 (508-638), A lid covering the substrate, 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,