Recombinant e.coli Dnak protein

MNEDEIQKMV RDAEANAEAD RKFEELVQTR NQGDHLLHST RKQVEEAGDK LPADDKTAIE SALTALETAL KGEDKAAIEA KMQELAQVSQ KLMEIAQQQH AQQQTAGADA SANNAKDDDV VDAEFEEVKD KK

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

E.coli

Heat Shock Proteins

14.6 kDa (132aa)