Human ERO1-Like (S. Cerevisiae) (ERO1L) Protein
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Description
Human ERO1-Like Protein is a recombinant protein from Human produced in Human Cells. Recombinant Human ERO1-Like Protein alpha is produced by our Mammalian expression system and the target gene encoding Glu24-His468 is expressed with a 6His tag at the C-terminus.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | ERO1-Like |
| Host | Human |
| Origin | Human |
| Observed MW | Molecular Weight: 53 kDa Sequence Fragment: Glu24-His468 Tag: C-terminal 6 His tag |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Form | Lyophilized |
| Tested Applications | SDS-PAGE |
| Buffer | 20mM PB, 150mM NaCl, pH7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Store at < -20°C. |
| Dry Ice | No |
| UniProt ID | Q96HE7 |
| Background | Protein ERO1L |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.
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