Description
Hsp90beta1, a member of the Hsp90 family of molecular chaperones, is involved in maintaining protein homeostasis in the secretory pathway and in intracellular trafficking of peptides from the extracellular space to the MHC class I antigen-processing pathway of antigenpresenting cells. Hsp90beta1 has key roles in signal transduction, protein folding, and protein degradation. It associates with several co-chaperones in folding of newly synthesized proteins and refolding of denatured proteins after stress. Hsp90beta1 is highly expressed in human gastric carcinoma BGC-823 cells throughout the cell cycle.
Recombinant human Hsp90 produced in E. coli is a single, non-glycosylated polypeptide containing 819 amino acids (aa 22-803) with a molecular weight of 94.4kDa. It is expressed with a 37 amino acid His-tag at the N-terminus