Human Coatomer Subunit Epsilon (COPE) Protein

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Description
Human Coatomer Subunit Epsilon (COPE) Protein is a recombinant protein expressed in E. coli.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Coatomer Subunit Epsilon (COPE) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 2 µg |
| Size 2 | 10 µg |
| Size 3 | 100 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Dry Ice | No |
| UniProt ID | O14579 |
| Gene ID | 11316 |
| NCBI Accession | NP_009194.2, NM_007263.3 |
| OMIM | 606942 |
| Background | Protein COPE |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors(ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors(By similarity).
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The product of this gene is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles. It is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Coatomer complex consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.
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