PDIA2
PDIA2 (protein disulfide isomerase family A member 2) is an endoplasmic reticulum lumen enzyme of the protein disulfide isomerase family that catalyses protein folding and thiol-disulfide interchange. It is also known as PDA2, PDI, PDIR and PDIP, and binds estradiol. Browse Assay Genie's current range of PDIA2 research reagents below, or read on for the biology behind the target.
PDIA2 is a member of the protein disulfide isomerase (PDI) family of endoplasmic reticulum proteins, which catalyse protein folding and thiol-disulfide interchange reactions. It contributes to the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds, using thiol isomerase, oxidase and reductase activities. UniProt also notes that it may act as a chaperone that inhibits aggregation of misfolded proteins.
Beyond its folding role, PDIA2 acts as an intracellular oestrogen-binding protein. It possesses estradiol-binding activity and can modulate intracellular estradiol levels, and it may be involved in modulating cellular levels and biological functions of oestrogens in the pancreas. This combination of folding catalysis and hormone binding distinguishes it within the family.
The PDIA2 gene encodes a protein with an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence, which keeps it in the endoplasmic reticulum lumen. HGNC places it in the protein disulfide isomerases gene group. Its previous names, including protein disulfide isomerase, pancreatic, and protein disulfide isomerase-associated 2, are reflected in the aliases PDA2, PDI, PDIR and PDIP. The mouse ortholog is Pdia2.
PDIA2 forms disulfide bonds in nascent proteins through thiol isomerase, oxidase and reductase activities in the endoplasmic reticulum.
As an ER lumen protein with TRX domains and a retention sequence, it is relevant to studies of ER-resident folding machinery.
PDIA2 binds estradiol and can modulate intracellular estradiol levels, linking protein folding enzymes to oestrogen handling.
PDIA2 may modulate oestrogen function in the pancreas and may act as a chaperone that inhibits aggregation of misfolded proteins.
PDIA2 catalyses protein folding and thiol-disulfide interchange in the endoplasmic reticulum, forming disulfide bonds through thiol isomerase, oxidase and reductase activities. It also binds estradiol, can modulate intracellular estradiol levels, and may act as a chaperone that inhibits aggregation of misfolded proteins.
PDIA2 is also called PDA2, PDI, PDIR and PDIP. Earlier names include protein disulfide isomerase, pancreatic, and protein disulfide isomerase-associated 2. UniProt lists the protein as protein disulfide-isomerase A2, and the enzyme carries the EC number 5.3.4.1.
A mouse ortholog, Pdia2, is recorded for the human PDIA2 gene. PDIA2 belongs to the wider protein disulfide isomerase family, whose members share thioredoxin-type domains. Check the datasheet of any product for its validated reactivity.
Other protein disulfide isomerase family members and endoplasmic reticulum folding enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q13087; product specifications from Assay Genie datasheets.