- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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PDIA3 Antibody / Protein Disulfide-Isomerase A3 Antibody recognizes PDIA3, an endoplasmic reticulum oxidoreductase also widely known as ERp57 and GRP58. PDIA3 belongs to the protein disulfide isomerase family and participates in the formation, reduction and rearrangement of disulfide bonds during protein folding. Within the ER, PDIA3 works closely with the lectin chaperones calnexin and calreticulin to promote the proper folding and maturation of newly synthesized glycoproteins. These functions place PDIA3 within the cellular machinery responsible for ER protein quality control and proteostasis.
PDIA3 contains multiple thioredoxin-like domains, including catalytically active domains containing CXXC motifs that mediate thiol-disulfide exchange reactions. Its association with calnexin and calreticulin helps direct PDIA3 toward glycoprotein substrates undergoing maturation in the ER lumen. By facilitating correct disulfide bond formation, PDIA3 contributes to the production of properly folded proteins capable of progressing through the secretory pathway. Misfolded proteins may instead be retained for additional folding attempts or directed toward degradation, connecting PDIA3 with broader mechanisms that maintain protein homeostasis.
Protein Disulfide-Isomerase A3 also has an important role in antigen processing and presentation. PDIA3 is a component of the MHC class I peptide-loading complex together with calreticulin, tapasin and other proteins involved in assembling peptide-MHC class I complexes. Within this machinery, PDIA3 contributes to the stability and function of the peptide-loading complex as antigenic peptides are selected for presentation at the cell surface. A PDIA3 Antibody can therefore support studies spanning ER protein quality control, antigen processing and molecular mechanisms involved in immune recognition.
Although PDIA3 is strongly associated with the endoplasmic reticulum, its reported biology extends beyond its classical role as an ER folding catalyst. PDIA3 has been detected in additional cellular compartments and investigated in signaling, cellular stress responses and protein-protein interactions. Altered PDIA3 expression or function has been studied in cancer, neurological disease and other conditions associated with disturbances in protein homeostasis. Its involvement in multiple cellular processes makes careful evaluation of tissue, cell type and subcellular localization important when studying PDIA3 experimentally.
PDIA3 provides an important connection between protein folding, ER quality control and cellular responses to proteotoxic stress. Its oxidoreductase activity and cooperation with calnexin and calreticulin are central to glycoprotein maturation, while its participation in the MHC class I peptide-loading complex extends its relevance to antigen processing. These functions place PDIA3 within the broader cellular mechanisms that preserve protein quality and respond to disruptions in protein homeostasis. NSJ Bioreagents supplies antibodies to PDIA3 and other proteins involved in cellular stress and proteostasis. An PDIA3 Antibody can support research on Protein Disulfide-Isomerase A3, ER protein folding, disulfide bond formation, glycoprotein quality control and cellular stress responses.
For related targets involved in ER protein folding, quality control and proteostasis, explore our Endoplasmic Reticulum Antibodies page.
Optimal dilution of the PDIA3 Antibody / Protein Disulfide-Isomerase A3 Antibody should be determined by the researcher.
Amino acids RELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL of human PDIA3/ERp57 were used as the immunogen for the PDIA3 antibody.
After reconstitution, the PDIA3 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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