protein

HSP70/DnaK Protein, E. coli (P.pastoris, His)

HY-P71824

5 μg;10 μg;50 μg

115;185;480 USD

HSP70/DnaK Protein, E. coli (P.pastoris, His)

proteins

P. pastoris

5 μg;10 μg;50 μg

115;185;480 USD

The HSP70/DnaK protein is a molecular chaperone that primarily responds to stress, especially heat shock. It plays a crucial role in helping proteins fold correctly and prevent misfolding or aggregation during cellular stress. HSP70/DnaK Protein, E. coli (P.pastoris, His) is the recombinant E. coli-derived HSP70/DnaK protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of HSP70/DnaK Protein, E. coli (P.pastoris, His) is 638 a.a., with molecular weight of ~71.1 kDa.

E.coli

HSP70/DnaK protein functions as a molecular chaperone, primarily responding to stress conditions, such as heat shock. In times of cellular stress, this protein plays a crucial role in assisting the proper folding of other proteins, preventing misfolding or aggregation. The chaperone activity of HSP70/DnaK is especially vital for cellular homeostasis and survival under adverse environmental conditions, where maintaining the correct conformation of proteins becomes challenging. The protein's ability to recognize and assist in the refolding of misfolded or denatured proteins is essential for cellular resilience and the prevention of proteotoxicity induced by various stressors, particularly elevated temperatures.

dnaK; HSP70; Heat shock 70kDa protein; Heat shock protein 70

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against solution in 20 mM Tris-HC1, 0.5 M NaCl, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.