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8334-GT) in the alpha 3 arm of the trimannose core of N-glycans and transfers a second GlcNAc residue to the alpha 6 arm of the structure to generate product glycan M2. MGAT2 can tolerate core-6 fucose and its Cy5 derivatives." class="big_lightbox" target="_blank">
GL302). In the presence of rhMGAT2, the glycan was modified and a mobility shift was observed." class="big_lightbox" target="_blank">
The product of the MGAT2 gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complexN-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, ahydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. Mutations in this gene may lead tocarbohydrate-deficient glycoprotein syndrome, type II. The coding region of this gene is intronless. Transcriptvariants with a spliced 5' UTR may exist, but their biological validity has not been determined. (provided byRefSeq)
![Enzyme Activity MGAT2 [Unconjugated]](http://images.novusbio.com/images/10711-gt_recombinant-human-n-acetylglucosaminyltransferase2-mgat2-cf-enzyme-activity-2432021144446.jpg)
![SDS-Page MGAT2 [Unconjugated]](http://images.novusbio.com/fullsize/10711-gt_recombinant-human-n-acetylglucosaminyltransferase2-mgat2-cf-sds-page-243202114512.jpg)
![Enzyme Activity MGAT2 [Unconjugated]](http://images.novusbio.com/images/10711-gt_recombinant-human-n-acetylglucosaminyltransferase2-mgat2-cf-enzyme-activity-1242021105826.jpg)
