DnaK Human, His

Recombinant Human DnaK (Hsp70) is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. This recombinant protein contains 661 amino acids and is fused to a His-tag at the N-terminus, resulting in a total molecular weight of approximately 72.2 kDa . The His-tag facilitates purification through affinity chromatography, making it easier to isolate the protein from other cellular components.

Hsp70 proteins, including DnaK, are essential for maintaining cellular homeostasis. They assist in the proper folding of nascent and stress-denatured proteins, preventing aggregation and assisting in the refolding of misfolded proteins. This function is vital for cell survival under stress conditions, such as heat shock, oxidative stress, and exposure to toxins.

In addition to their role in protein folding, Hsp70 proteins are involved in various cellular processes, including:

• Protein translocation: Assisting in the transport of proteins across cellular membranes.
• Protein degradation: Targeting misfolded proteins for degradation via the ubiquitin-proteasome system.
• Signal transduction: Modulating signaling pathways related to stress responses.

Recombinant Human DnaK (Hsp70) with a His-tag is widely used in research and biotechnology. Some of its applications include:

• Protein folding studies: Investigating the mechanisms of protein folding and the role of chaperones.
• Stress response research: Studying cellular responses to various stress conditions.
• Drug discovery: Screening for compounds that modulate Hsp70 activity, which could lead to potential therapeutic agents for diseases related to protein misfolding and aggregation.

Recombinant Human DnaK (Hsp70) is typically stored at or below -20°C for long-term stability. For short-term storage, it can be kept at 4°C for up to four weeks. To enhance stability, the addition of a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), is recommended .