ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Greater than 95.0% as determined by SDS-PAGE.
PDIA3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 505 amino acids (25-505 a.a) and having a molecular mass of 56.8kDa.
PDIA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
MGSSHHHHHH SSGLVPRGSH MGSMSDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL QREATNPPII QEEKPKKKKK AQEDL.
PDIA3 is primarily localized in the endoplasmic reticulum (ER) due to its N-terminal signal peptide. However, it is ubiquitous within the cell, likely due to a noncanonical ER retention motif (QEDL) at the C-terminal, the presence of a nuclear localization sequence, and its capability to interact with a wide range of proteins . The enzyme catalyzes the rearrangement of -S-S- bonds in proteins, which is essential for proper protein folding and stability .
PDIA3 is a 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, PDIA3 assists in the dynamic assembly of the MHC I complex with high-affinity antigens in the ER. This process is crucial for the presentation of antigens to cytotoxic T cells in adaptive immunity .
PDIA3 has been implicated in various physiopathological processes, including cancer initiation, progression, and chemosensitivity. For instance, studies have shown that the inhibition or silencing of PDIA3 in glioblastoma cell lines can reduce cell spreading and increase chemosensitivity to the drug temozolomide . Additionally, PDIA3 is required for the oxidative folding of influenza A virus hemagglutinin, indicating its role in viral propagation .
Given its involvement in critical cellular processes and disease mechanisms, PDIA3 is considered a potential therapeutic target. Inhibiting PDIA3 functions could lead to cytotoxic effects in cancer cells and enhance the efficacy of existing treatments . Further research is needed to explore its therapeutic potential fully.