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.

P4HB; Pancreas specific protein disulfide isomerase; Pancreas-specific protein disulfide isomerase; Pancreatic protein disulfide isomerase; PDA2; PDI; PDIA2; PDIA2_HUMAN; PDIP; PDIR; Protein disulfide isomerase A2; Protein disulfide isomerase; Protein disulfide isomerase associated 2; Protein disulfide isomerase family A member 2; Protein disulfide isomerase pancreatic; Protein disulfide-isomerase A2; Rho GDP dissociation inhibitor gamma.

Rat,Human,Mouse

WB

WB 1:500-2000

56kD

64714

Q13087

https://www.uniprot.org/uniprotkb/Q13087

Endoplasmic reticulum lumen.

Highly expressed in pancreas (at protein level).

KLH conjugated synthetic peptide derived from human PDIA2

Rabbit

Polyclonal

IgG

affinity purified by Protein A

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.