Unconjugated Rabbit anti-Human, Mouse, Rat P4HB Monoclonal Antibody [IgG]

Cellular thyroid hormone binding protein antibody, Cellular thyroid hormone-binding protein antibody, Collagen prolyl 4 hydroxylase beta antibody, Disulphide Isomerase antibody, DSI antibody, EC 5.3.4.1 antibody, Endoplasmic reticulum resident protein 59 antibody, ER protein 59 antibody, ERBA2L antibody, ERp59 antibody, GIT antibody, Gltathione insulin transhydrogenase antibody, Glutathione insulin transhydrogenase antibody, P4HB antibody, P4Hbeta antibody, p55 antibody, PDI antibody, PDIA1 antibody, PDIA1_HUMAN antibody, PDIR antibody, PHDB antibody, PO4DB antibody, PO4HB antibody, Procollagen proline 2 oxoglutarate 4 dioxygenase (proline 4 hydroxylase) beta polypeptide (protein disulfide isomerase associated 1) antibody,

The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.