GRP78 antibody

The 78 kDa glucose-regulated protein (GRP78) is the eukaryotic orthologue to the prokaryotic heat shock 70 kDa protein 5 (HSPA5). GRP78 is also sometimes referred to as BiP. GRP78 is a member of the HSP70 family and plays dynamic roles in protein regulation within the endoplasmic reticulum. GRP78 is the most abundant chaperone in the ER and plays an important role in regulating the unfolded protein response (UPR) (1). GRP78 forms a multiprotein chaperone complex with DNAJB11, HSP90B1, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1, and ERP29.

HSP70 family member GRP78 (78 kD glucose-regulated protein) is an abundant protein cofactor commonly known as a molecular chaperone. Found in most eukaryotes, Hsp genes are members of a heat-inducible multigene family.