Qproteome Sialic Glycoprotein Kit
For specific enrichment of glycoproteins with sialic-acid-rich glycan moieties
The Qproteome Sialic Glycoprotein Kit contains three different lectin-resin-filled spin columns, buffers, and reagents for the isolation of glycoproteins with sialic-acid-rich glycan moieties from 6 cell lysate or serum samples.
The Qproteome Sialic Glycoprotein Kit enables highly specific enrichment of glycoproteins with sialic-acid-rich glycan moieties (see figure Highly specific glycoprotein fractionation). The selection of lectin columns allow accurate characterization of glycoproteins.
Proteins with sialic acid-rich glycan moieties bind to lectins immobilized on the resin in the spin columns. After washing, proteins are eluted by addition of an elution buffer containing sugars which compete for lectin binding sites with the bound proteins.
The sample is diluted and applied to the spin column (see figure Glycoprotein fractionation procedure). After a short incubation, proteins that have not bound to the lectin are removed by centrifugation. Bound proteins are eluted by application of elution buffer and centrifugation.
Glycosylation plays a vital role in a wide range of cellular processes such as cell adhesion and signaling, stabilization of protein structure and function, protein trafficking and sorting, and oncogenesis. Several diseases (e.g., rheumatoid arthritis, muscular dystrophy) may be caused by a defect in protein glycosylation. Qproteome Glycoprotein Fractionation Kits offer highly specific separation of glycoproteins according to the structure of their glycan moieties, and permit profiling of glycoproteins in cells grown under different conditions.
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