Recombinant E. coli HSP70/HSPA1A Protein

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.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Array NBC1-18358

• HSP70/HSPA1A Antibodies
• HSP70/HSPA1A Lysate
• HSP70/HSPA1A Proteins
• HSP70/HSPA1A ELISAs
• HSP70/HSPA1A Proteins and Enzyme