Human, DnaK Human Recombinant Protein, His Tag

HSP 70kDa produced in E.Coli is a single, non-glycosylated polypeptide chain (1-641 a.a.) containing 661 amino acids fused to a 20 a.a. His-tag at N-terminus and having a total Mw of 72.2 kDa.

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).

Shipped with wet ice

Store in -20° C for long term storage. After reconstitution, store in 4° C for short term usage within a few days. Avoid freeze-thaw cycles.

HSPA1B is testis-specific.