Qproteome O-Glycan Glycoprotein Kit

For specific enrichment of glycoproteins with a glycan structure of the type that are found on T-antigens
  • Specific separation of glycoproteins according to their glycan moieties
  • Glycoprotein profiling in cells grown under different conditions or in different disease states
  • Comprehensive glycoprotein characterization
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.

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Qproteome O-Glycan Glycoprotein Kit
For 6 O-glycan glycoprotein preps: AIL and PNA Lectin Spin Columns (3 each); Buffers; Protease Inhibitor Solution; Collection Tubes (6 x 2 ml)
37571
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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.
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Glycoprotein fractionation procedure.|Highly specific glycoprotein fractionation.|
|Glycoproteins were fractionated from serum using the different lectin spin columns in glycoprotein fractionation kits and analyzed by SDS-PAGE followed by silver staining. [A] Elution steps 1–3 and 4–6 from Total Lectin Spin Columns in the Total Glycoprotein Kit. [B] Eluted glycoproteins from ConA, GNA, and LCH Spin Columns in the Mannose Glycoprotein Kit. [C] Eluted glycoproteins from WGA, SNA, and MAL Spin Columns in the Sialic Glycoprotein Kit. [D] Eluted glycoproteins from AIL and PNA Spin Columns in the O-Glycan Glycoprotein Kit.|
Performance
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.
Principle
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.
Procedure
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.
Applications
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.
Feature
Specifications
Applications SDS-PAGE, mass spectrometry
Binding capacity/yield 30–150 µg
For glycoproteins: which type of glycoproteins Glycoproteins with a glycan structure
Fractions isolated One fraction
Protein with post-translational modification Glycosylation
Sample size 50 µl
Start material Serum

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