Anti-ERp57 (GRP58) Monoclonal Antibody

ERp57, also known as Glucose Regulated Protein 58 (Grp58), Hormone-Induced Protein-70 (HIP-70) and microsomal Carnitine Palmitoyltransferase, is a member of the protein disulfide isomerase family, containing two canonical CXHC tetrapeptide active site motifs (1-5) . It has quite a few diverse roles. It functions as an accessory oxidoreductase involved in disulfide bond formation. In the ER, ERp57 interacts with membrane bound calnexin and soluble calreticulin (lectin chaperones) via their praline rich P-domain arms. Lectin chaperones bind nascent non-native glycoproteins, and position ERp57 to act upon the immature or misfolded glycoproteins that possess mono-glycosylated side chains. ERp57 deletion impairs posttranslational phases of influenza hema-glutinin folding, and causes accelerated release of MHC-I molecules, resulting in the coupling of sub-optimal peptides and reduced expression and stability on the cell surface (6) . ERp57 also contains two thioredoxin active-site sequences, CGHC and an estrogen-binding domain. ERp57 is induced by both estrogen and leuteinizing-hormone-releasing hormone in the hippocampus (7) .

ERp60, ERp61, Grp57, Grp58, P58, PDIA3, PI PLC, 58 kDa glucose regulated protein, 58 kDa glucose-regulated protein, 58 kDa microsomal protein, Disulfide isomerase ER 60, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 57, Endoplasmic reticulum resident protein 60, ER p57, ER protein 57, ER protein 60, ERp 57, ERp57, Glucose Regulated Protein 58 Kd, GRP 57, GRP 58, GRP57, HsT17083, p58, PDIA 3, PDIA3, PDIA3_HUMAN, Phospholipase C alpha, PI PLC, Protein disulfide isomerase A3, Protein disulfide isomerase family A member 3, Protein disulfide-isomerase A3