E. coli HSP70 (aa 1 - 638), recombinant protein from E. coli
Escherichia coli dnaK (NP_414555, a.a. 1-638) full-length recombinant protein expressed in Escherichia coli.
Please see the vial label for concentration
In 25 mM Tris-HCl, 100 mM NaCl, pH 7.5 (5 mM DTT, 10% glycerol)
2-8°C short term, -20°C long term
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.
The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress.
DAQB 147D11.1 001; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A/1B; heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; Heat shock induced protein; heat sh