Lu, Grace published the artcileProfiling the N-Glycan Composition of IgG with Lectins and Capillary Nanogel Electrophoresis, Recommanded Product: (2R,3S,4S,5R)-2,3,4,5,6-Pentahydroxyhexanal, the main research area is IgG glycan profiling lectin capillary nanogel electrophoresis.
Glycosylated human IgG contains fucosylated biantennary N-glycans with different modifications including N-acetylglucosamine, which bisects the mannose core. Although only a limited number of IgG N-glycan structures are possible, human IgG N-glycans are predominantly biantennary and fucosylated and contain varying levels of α2-6-linked sialic acid, galactose, and bisected N-acetylglucosamine. Monitoring the relative abundance of bisecting N-acetylglucosamine is relevant to physiol. processes. A rapid, inexpensive, and automated method is used to successfully profile N-linked IgG glycans and is suitable to distinguish differences in bisection, galactosylation, and sialylation in N-glycans derived from different sources of human IgG. The separation is facilitated with self-assembled nanogels that also contain a single stationary zone of lectin. When the lectin specificity matches the N-glycan, the peak disappears from the electropherogram, identifying the N-glycan structure. The nanogel electrophoresis generates separation efficiencies of 500 000 plates and resolves the positional isomers of monogalactosylated biantennary N-glycan and the monogalactosylated bisected N-glycan. Aleuria aurantia lectin, Erythrina cristagalli lectin (ECL), Sambucus nigra lectin, and Phaseolus vulgaris Erythroagglutinin (PHA-E) are used to identify fucose, galactose, α2-6-linked sialic acid, and bisected N-acetylglucosamine, resp. Although PHA-E lectin has a strong binding affinity for bisected N-glycans that also contain a terminal galactose on the α1-6-linked mannose branch, this lectin has lower affinity for N-glycans containing terminal galactose and for agalactosylated bisected biantennary N-glycans. The lower affinity to these motifs is observed in the electropherograms as a change in peak width, which when used in conjunction with the results from the ECL lectin authenticates the composition of the agalactosylated bisected biantennary N-glycan. For runs performed at 17°, the precision in migration time and peak area was less than or equal to 0.08 and 4% relative standard deviation, resp. The method is compatible with electrokinetic and hydrodynamic injections, with detection limits of 70 and 300 pM, resp.
Analytical Chemistry (Washington, DC, United States) published new progress about Aleuria aurantia. 59-23-4 belongs to class alcohols-buliding-blocks, name is (2R,3S,4S,5R)-2,3,4,5,6-Pentahydroxyhexanal, and the molecular formula is C6H12O6, Recommanded Product: (2R,3S,4S,5R)-2,3,4,5,6-Pentahydroxyhexanal.
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