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LFNG Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q8NES3 |
|---|
| Gene ID | 3955 |
|---|---|
| Other Names | Beta-1, 3-N-acetylglucosaminyltransferase lunatic fringe, O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, LFNG |
| 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 | LFNG (HGNC:6560) |
|---|---|
| Function | Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O- fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (PubMed:11346656). Essential mediator of somite segmentation and patterning (By similarity). |
| Cellular Location | Golgi apparatus {ECO:0000250|UniProtKB:O09010}. Golgi apparatus membrane; Single-pass type II membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
LFNG belongs to evolutionarily conserved glycosyltransferases that act in the Notch signaling pathway to define boundaries during embryonic development. While their genomic structure is distinct from other glycosyltransferases, fringe proteins have a fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity that leads to elongation of O-linked fucose residues on Notch, which alters Notch signaling. This protein is predicted to be a single-pass type II Golgi membrane protein but it may also be secreted and proteolytically processed like the related proteins in mouse and Drosophila (PMID: 9187150).
References
Dunwoodie, S.L. Biochim. Biophys. Acta 1792(2):100-111(2009) Reedijk, M., et al. Int. J. Oncol. 33(6):1223-1229(2008) Sparrow, D.B., et al. Am. J. Hum. Genet. 78(1):28-37(2006) Cole, S.E., et al. Dev. Cell 3(1):75-84(2002) Moran, J.L., et al. Mamm. Genome 10(6):535-541(1999)
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