Description
Product Characteristics:
Endoplasmic reticulum proteins (ERps) are widely expressed proteins and localize to the ER. ERp19, ERp29, ERp46, ERp57 and ERp72 may act as proteases, protein disulfide isomerases, thiol-disulfide oxidases, phospholipases or a combination of these. ERp19, also designated thioredoxin domain-containing protein 12 (TXNDC12), and ERp46, also designated thioredoxin domain containing 5 (TXNDC5), belong to the thioredoxin superfamily and contain a thioredoxin fold with a consensus active-site sequence (CxxC). Both ERp19 and ERp46 are widely expressed ER luminal proteins that are most abundant in the liver and are enriched in purified liver ER vesicles. ERp19 shows significant protein thiol-disulfide oxidase activity in vitro, which is dependent on the presence of both active-site cysteines.
Subcellular location: Cytoplasm
Synonyms: AG1, AGR1, anterior gradient homolog 1, endoplasmic reticulum protein ERp19, endoplasmic reticulum resident protein 18, endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member, 18 kDa, ER protein 18, ER protein 19, ERP 18, ERP16, ERP19, hAG 1, hAG1, hTLP19, PDIA16, protein disulfide isomerase family A, member 16, thioredoxin domain containing 12 endoplasmic reticulum, Thioredoxin domain-containing protein 12, thioredoxin like protein p19, TLP19, TXNDC12, TXD12_HUMAN.
Target Information: This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. This protein localizes to the endoplasmic reticulum and has a single atypical active motif. The encoded protein is mainly involved in catalyzing native disulfide bond formation and displays activity similar to protein-disulfide isomerases. This protein may play a role in defense against endoplasmic reticulum stress. Alternate splicing results in both coding and non-coding variants. [provided by RefSeq, Mar 2012]