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MPDU1 Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O75352 |
|---|---|
| Other Accession | MPU1_HUMAN |
| Clone Names | 3102201 |
| Gene ID | 9526 |
|---|---|
| Other Names | Mannose-P-dolichol utilization defect 1 protein, Suppressor of Lec15 and Lec35 glycosylation mutation homolog, SL15, MPDU1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2408a was selected from the Center region of human MPDU1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | MPDU1 |
|---|---|
| Function | Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors. |
| Cellular Location | Membrane; Multi-pass membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glycosylation is one of the most universal but at the same time complex protein modifications. Modification with sugar moeties can be both co- translational and post- translational, occurring in the endoplasmatic reticulum and golgi. Three different forms of glycosylation can be distinguished: N-linked oligosaccharides, O-linked oligosaccharides and glycosyl- phosphatidylinositol (GPI-) anchors. Glycosylation results in thousands of distinct, bioactive glycoproteins resident throughout the cell that strongly determine protein-protein, carbohydrate-protein, membrane, and adhesion properties. Diseases associated with glycosylation defects include Congenital disorders of glycosylation, (CDG), also known as carbohydrate deficient glycoprotein syndromes, and diseases associated with advanced aging.
References
Mao, M., et al., Proc. Natl. Acad. Sci. U.S.A. 95(14):8175-8180 (1998).Ware, F.E., et al., J. Biol. Chem. 271(24):13935-13938 (1996).
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