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Overview
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HSP90B1 produced in E. Coli is a single, non-glycosylated polypeptide chain containing 819 amino acids (22-803 a.a.) and having a molecular mass of 94.4 kDa. HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques. 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.
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Overview