Endoplasmic reticulum oxidoreductase 1-like protein alpha (ERO1L alpha) is an FAD-dependent protein disulfide oxidase. Disulfide bond formation in the mammalian endoplasmic reticulum relies on the combined activity of ERO1L and protein disulfide isomerase (PDI), the enzyme responsible for catalyzing protein disulfide formation. During the formation of disulfide bonds, ERO1L concurrently produces hydrogen peroxide, making it a source of reactive oxygen species production. There are two mammalian homologues of ERO1 that share 65% sequence identity; ERO1L alpha is more widely expressed, while ERO1L beta is present in select tissues. Both homologues contain two essential conserved cysteine triads. The N-terminal triad is involved in interaction with PDI, whereas the C-terminal triad forms an active site near FAD. Both homologues are regulated by the formation of disulfide bonds within the active site cysteines, but whereas ERO1L beta is loosely regulated, enzyme activity of ERO1L alpha is tightly controlled. ERO1L alpha has been shown to be critical in hepatic stellate cell proliferation, making it a potential target for managing liver fibrosis. ERO1L alpha knockdown inhibits cell proliferation, migration, invasion, and chemoresistance, while overexpression promotes tumor growth and angiogenesis. ERO1L alpha is overexpressed in various types of tumors including breast, gastric, and colon cancer, where its up-regulation correlates to a poor prognosis. ERO1L alpha has been proposed to be a clinically promising therapeutic target for ERO1L-expressed cancers.
Post-translational: N-glycosylated. The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870). Phosphorylated on Ser-145 by FAM20C in the Golgi which increases its enzymatic activity (PubMed:29858230). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (PubMed:29858230).
52.0 kDa, under reducing conditions; 46.9 & 49.8 & 102.3 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
液体
储存缓冲液
20mM Tris, 10% Glycerol, pH 8.0
浓度
见COA
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
Store at -20°C for 1 year. Avoid freeze/thaw cycle.
图片
Recombinant Human ERO1L alpha Protein (rp188318) - SDS-PAGE 3 μg/lane of Recombinant Human ERO1L alpha Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 52.0 kDa under reducing conditions and 46.9 & 49.8 & 102.3 kDa under non-reducing conditions.
ZJ25F0116487
危险品化学品经营许可证（带存储）