Anti-Human ERp57 Antibody Pair

Product Description: Protein disulfide isomerase family A member 3 (PDIA3) is an endoplasmic reticulum-resident thiol oxidoreductase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in newly synthesized proteins, ensuring their proper folding and structural stability. PDIA3 interacts with lectin chaperones such as calreticulin and calnexin, playing a crucial role in the calnexin/calreticulin cycle and the assembly of the major histocompatibility complex (MHC) class I peptide loading complex, which is essential for antigen presentation. It also acts as a redox sensor, modulating cell growth and death in response to oxygen levels, and participates in cytoskeletal organization and cytokine-dependent signaling pathways, including STAT3 signaling. Beyond its protein-folding functions, PDIA3 is upregulated during cellular stress and is implicated in diseases such as cancer, where its elevated expression is associated with tumor progression, and in viral infections, where it facilitates viral entry and replication. Protein Function: Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323) [The Uniprot Consortium]