Greater than 85.0% as determined by SDS-PAGE.
DnaK, also known as HSP70, is a highly conserved molecular chaperone found in Escherichia coli (E. coli). It plays a crucial role in protein homeostasis by assisting in the folding of newly synthesized polypeptides, preventing the aggregation of misfolded proteins, and aiding in the refolding of stress-denatured proteins .
DnaK is a member of the HSP70 family of heat shock proteins, which are characterized by their ability to bind and hydrolyze ATP. The protein consists of three main domains:
The ATPase activity of DnaK is essential for its function as a chaperone. The binding and hydrolysis of ATP induce conformational changes in DnaK, allowing it to interact with substrate proteins and facilitate their proper folding .
In E. coli, DnaK is involved in various cellular processes, including:
Recombinant DnaK is produced by cloning the dnaK gene from E. coli into an expression vector and expressing the protein in a suitable host system. This allows for the production of large quantities of DnaK for research and industrial applications. Recombinant DnaK retains the functional properties of the native protein and is used in studies related to protein folding, stress response, and chaperone activity .
Recombinant DnaK has several applications in research and biotechnology: