Human HSP70/HSPA1A (His Tag) recombinant protein

Human HSP70/HSPA1A (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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). {PubMed:16537599, PubMed:22528486, PubMed:23973223}.

Heat shock 70 kDa protein 1B

P0DMV9

HSPA1B

Baculovirus-Insect Cells

A DNA sequence encoding the human HSPA1A (NP_005337.2) (Ala2-Asp641) was expressed, with a polyhistidine tag at the N-terminus.

Human

The recombinant human HSPA1A consists of 658 amino acids and predicts a molecular mass of 72.2 kDa.

> 85 % as determined by SDS-PAGE

1. Measured by its ability to bind human PARP1 in a functional ELISA.
2. Measured by its ability to bind mouse PARP1 in a functional ELISA.