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HSP90 proteins are highly conserved molecular chaperones, which normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 (GP96 or GRP94) is an endoplasmic reticulum paralogue of the cytosolic HSP90. As a major ER chaperone to mediate the UPR and a master chaperone for Toll-like receptors (TLRs), HSP90b1 chaperones peptides to MHC class I molecules of dendritic cells and other antigen-presenting cells, as well as facilitating the assembly of immunoglobulin. The protein is also involved in many other bio-processes. This antibody was generated against the N-terminal region of full-length HSP90b1.