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Biotech Support Group Release: Glycoprotein Enrichment to Complement Chromatographic Separation and Glycoprotein Profiling


9/16/2013 9:22:13 AM

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PRLog (Press Release) - Sep. 15, 2013 - MONMOUTH JUNCTION, N.J. -- MONMOUTH JUNCTION, N.J. - Eliminating sample complexity by enriching glycosylated proteins enhances downstream biotechniques such as mass spectrometry. Coupling glycoprotein enrichment techniques with multidimensional chromatographic separation could allow for glycoprotein profiling and biomarker discovery. NuGel™ Glycoprotein Enrichment PBA Kit - With Phenyl Boronic Acid NuGel™ Matrix unmasks glycoproteins from high abundance proteins, is cis-diol specific and enriches glycoproteins from blood, serum, plasma, tissue or cell culture media. With NuGel™, non-specific sites have been virtually eliminated making it an ideal support for affinity purification. The Phenyl Boronic Acid (PBA) ligand is immobilized through the NuGel™ poly-Epoxy linkage with attachment through the amino group. While various lectins bind to specific saccharide residues, the PBA ligand binds to the 1,2-cis-diol groups of biomolecules and enriches for heterogeneous sets of glycoproteins containing both N-linked and O-linked oligosaccharides. An easy and fast spin-filter format makes glycoprotein enrichment simple starting from 50µl serum, or 1-2 mg total protein.

Applications of NuGel™ Glycoprotein Enrichment PBA Kit - With Phenyl Boronic Acid NuGel™ Matrix

- Structural characterization of N- and O-linked carbohydrates attached to proteins.

- Mass spectrometry proteomic analysis of glycan structures, glycoproteins, peptide sequence, glycan attachment site and glycan structure. Identify genes encoding glycoproteins and glycosylation sites

- Subsequent to enrichment research on sites of O-GlcNAc modification on proteins of low abundance provides information on mutagenesis and oncogenes.

- Separation of N- and O-linked glycans from glycoproteins on sodium dodecyl sulfate polyacrylamide electrophoresis gels

- Glycan profile characterization via matrix-assisted laser desorption/ionization mass spectrometry

- Conduct proteomic research on post translational modification and intracellular, cell-cell and cell-matrix events.

- Identify genes encoding glycoproteins and glycosylation sites.

- Recombinant immuno-globulins (rIgG) research.

- Complements lectin-affinity chromatography, frontal affinity chromatography and contemporary in silico database searching

For more information on NuGel™ Glycoprotein Enrichment PBA Kit - With Phenyl Boronic Acid NuGel™ Matrix: http://biotechsupportgroup.com/node/260

About Biotech Support Group LLC

Biotech Support Group LLC is a leading provider of genomics and proteomics sample preparation products and enrichment reagent kits as well as integrated biotechnology services for life sciences research, biomarker and drug discovery. Based in New Jersey, it’s principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ for lipid adsorption and clarification, NuGel™ for passivated silica-based affinity chromatography, and ProCipitate™ & ProPrep™ for nucleic acid isolation. Currently, Biotech Support Group LLC and ProFACT Proteomics Inc., are collaborating on the development of a proteomics platform used in functional profiling for proteomic analysis and a separations method for generating sub-proteomes used in biomarker and functional proteomic prospecting. For more information, go to: www.biotechsupportgroup.com

CONTACT:

Dr.Swapan Roy

Biotech Support Group

1 Deer Park Drive, Suite M,

Monmouth Junction, NJ 08852, USA

732-274-2866

sales@biotechsupportgroup.com

Suggested References

Harvey, David J. "Structural determination of N-linked glycans by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry." Proteomics 5.7 (2005): 1774-1786.

Raju, T. Shantha, et al. "Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics."Glycobiology 10.5 (2000): 477-48

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