heat shock 70kD protein 6 (HSP70B); heat shock 70kDa protein 6 (HSP70B)
Amino Acid Labeled
[U- 13C6, 15N4]-L-Arg and [U- 13C6, 15N2]-L-Lys
> 80% as determined by SDS-PAGE and Coomassie blue staining
Human HEK293 cells
Expression TrueORF Clone
HSPA6 Full-Length MS Protein Standard (NP_002146), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. 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.