|Other Names||Beta-1, 3-N-acetylglucosaminyltransferase lunatic fringe, O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase, LFNG|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|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.|
|Function||Glycosyltransferase that initiates the elongation of O- linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Decreases the binding of JAGGED1 to NOTCH2 but not that of DELTA1. Essential mediator of somite segmentation and patterning (By similarity).|
|Cellular Location||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.
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).
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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