% SDS-PAGE. Purified by multi-step chromatography.
>90% pure as determined by SDS-PAGE and Western blot analyses.
This protein does not contain DnaK as demonstrated by western blot analysis.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
DnaK type molecular chaperone HSP70 1
Epididymis secretory protein Li 103
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
HEL S 103
FunctionIn 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.
Tissue specificityHSPA1B is testis-specific.
Sequence similaritiesBelongs to the heat shock protein 70 family.
Cellular localizationCytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs.