Recombinant Human ERO1L alpha Protein

重组人ERO1L Alpha蛋白 | 重组人内质网氧化还原酶1α蛋白

EC 1.8.4 | EC 1.8.4.- | Endoplasmic oxidoreductin-1-like protein | ERO1 (S. cerevisiae)-like | ERO1A | ERO1-alpha | ERO1L alpha | ERO1-l alpha | ERO1L | ERO1-L | ERO1-L-alpha | ERO1-like (S. cerevisiae) | ERO1-like alpha | ERO1-like protein alpha | ERO1-l

rp188318-10μg

10μg

无载体

≥95%(SDS-PAGE)

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).

重组表达

52.9 kDa

N-His

52.0 kDa, under reducing conditions; 46.9 & 49.8 & 102.3 kDa, under non-reducing conditions.

E. coli Accession #: Q96HE7 | E. coli

<1.0 EU/μg

人(Human)

24-468 aa

MHHHHHHEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH

No

Yes