ERO1L Recombinant Protein Antigen

Perhaps the most distinctive feature of protein folding in the ER is the abundance of disulfide bonds that must form during maturation of proteins traveling along the secretory pathway. Formation of disulfide bonds is a redox reaction. Thus, to match the flux of disulfide bonds that exit from the ER by virtue of protein secretion, a flux of oxidizing equivalents into the ER is required. In eukaryotic cells, the essential protein relay supporting this flux, and hence disulfide bond formation, involves endoplasmic reticulum oxidoreductin 1 (Ero1) and protein disulfide isomerase (PDI). The temporal pattern of hypoxic ERO1-L alpha induction is very similar to that of genes triggered by the hypoxia inducible transcription factor (HIF-1) and is characteristically mimicked by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor translocator (ARNT, HIF-1 alpha). We speculate from these findings that the expression of ERO1-L alpha is probably regulated via the HIF-pathway and thus belongs to the family of classic oxygen regulated genes.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Array NBP1-84800PEP

• ERO1L Antibodies
• ERO1L Lysate
• ERO1L Proteins
• ERO1L Proteins and Enzyme