GPLD2 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P80108 |
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Other Accession | Q15127 |
Gene ID | 2822 |
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Other Names | Phosphatidylinositol-glycan-specific phospholipase D, PI-G PLD, Glycoprotein phospholipase D, Glycosyl-phosphatidylinositol-specific phospholipase D, GPI-PLD, GPI-specific phospholipase D, GPLD1, PIGPLD1 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2461a was selected from the N-term region of human GPLD2 . 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 | GPLD1 |
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Synonyms | PIGPLD1 |
Function | This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. |
Cellular Location | Secreted. |
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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
Tsang, T.C., et al., FASEB J. 6, A1922-A1922 (1992).
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