Application

Anti-Protein Disulfide Isomerase (DL-11) antibody produced in rabbit has been used in: immunofluorescence immunoprecipitation immunoblotting

Biochem/physiol Actions

Protein Disulfide Isomerase serves as a molecular chaperone, that can suppress protein aggregation. PDI has functions as an essential component of two protein complexes: the heterotetramer collagen prolyl 4-hydroxylase and the heterodimer microsomal triglyceride transfer protein. PDI participates in the hydroxylation of prolines in procollagen during collagen synthesis and in the transfer of neutral lipid onto nascent lipoprotein particles. PDI has calcium-dependent transglutaminase activity, which catalyzes the formation of isopeptide bonds.

Prolyl 4-hydroxylase subunit β (P4HB) acts as a molecular chaperone in the endoplasmic reticulum of cells and also as an oxidoreductase. It associates with steroid hormones and modulates their actions, concentrations and storage. P4HB accelerates the formation of disulphide bonds in proteins and hence aids in their folding.

Disclaimer

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General description

Prolyl 4-hydroxylase subunit β (P4HB) is a redox-regulated thiol-containing protein. The gene encoding this protein is localized on human chromosome 17q25.3.

Protein Disulfide Isomerase is an abundant multifunctional, soluble enzyme (E.C. 5.3.4.1). PDI is expressed in cellular localizations such as the cell surface, cytosol and nucleus. PDI consists of four tandem domains, two of which contain a catalytic site for S-S bond formation. One domain is the main site of noncovalent interaction with other peptides or proteins. PDI has an N-terminal ER signal and C-terminal ER retention KDEL signal sequences.

Immunogen

synthetic peptide corresponding to amino acid residues 498-508 of human protein disulfide isomerase.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.