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We conclude that ERp19 contributes to tumorigenicity and metastasis of gastric cancer
ERp18 shows specificity towards a component of the complement cascade, pentraxin-related protein PTX3.
putative physiological role for endoplasmic reticulum thioredoxin superfamily member p18(ERp18) in native disulfide bond formation is discussed
ERp16 mediates disulfide bond formation in the ER and plays an important role in cellular defense against prolonged ER stress
the solution structure of oxidized ERp18 as determined using NMR spectroscopy
both ERp19 and ERp46 and their respective mRNAs are highly expressed in the liver as compared with other tissues
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.
ER protein 18
, ER protein 19
, 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
, protein disulfide isomerase family A, member 16
, thioredoxin domain-containing protein 12
, thioredoxin-like protein p19
, ortholog of endoplasmic reticulum thioredoxin superfamily member, 18 kDa TLP19