Heat Shock Protein gp96 (gp96)

Heat Shock Protein gp96 (gp96), also known as grp94, endoplasmin, ERp99, or HSP90B1, is a member of the HSP90 family of molecular chaperones primarily localized in the endoplasmic reticulum (ER). It functions as a dimeric glycoprotein that assists in the folding, maturation, and quality control of newly synthesized proteins within the ER. gp96 binds peptides noncovalently, a property crucial for its role in antigen presentation and immune activation. It plays a pivotal role in both innate and adaptive immunity by chaperoning antigenic peptides for cross-presentation and activating dendritic cells. Dysregulation is implicated in various cancers, and it is explored as a target for cancer immunotherapy.

Other names

grp94endoplasminERp99HSP90B1

gp96-peptide complexes are used in autologous cancer vaccines to stimulate anti-tumor immunity by presenting tumor-specific antigens to T cells, leading to cytotoxic T-cell responses.