Recombinant Human Heat Shock Protein 90kDa Beta (GRP94) Member 1, HEK

Source : HEK 293. HSP90B1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asp22-Glu798) containing a total of 789 amino acids, having a calculated molecular mass of 90.9kDa. HSP90B1 is fused to a 2 aa N-terminal linker, a 4 aa C-terminal linker and a 6 aa His tag at C-Terminus. HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.