Qproteome O-Glycan Glycoprotein Kit
For specific enrichment of glycoproteins with a glycan structure of the type that are found on T-antigens
The Qproteome O-Glycan Glycoprotein Kit contains two different lectin-resin-filled spin columns, buffers, and reagents for the isolation of glycoproteins with a glycan structure of the type that are found on T-antigens from 6 cell lysate or serum samples. The kit can be automated on the QIAcube Connect.
The Qproteome O-Glycan Glycoprotein Kit is intended for molecular biology applications. This product is not intended for the diagnosis, prevention, or treatment of a disease.
The Qproteome O-Glycan Glycoprotein Kit enables highly specific enrichment of glycoproteins with a glycan structure of the type that are found on T-antigens (see figure Highly specific glycoprotein fractionation). Glycoprotein profiling of cells grown under different conditions or in different disease states can be carried out reliably. The selection of lectin columns allow precise glycoprotein characterization.
Glycosylated proteins with a glycan structure of the type that are found on T-antigens 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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