MINNEAPOLIS, Sept. 6, 2018 /PRNewswire/ -- Bio-Techne researchers publish papers that promise to open the field of glycobiology to the masses.
Sugars, also known as glycans, are attached to many proteins found both inside and on the surface of cells. This modification of proteins is called glycosylation. Because glycans have been tied to many pathologies, ranging from cancer to neurodegenerative disease, it is important to better understand their structures and functions. Unfortunately, glycobiology has been difficult to study as current techniques often suffer from a lack of specificity or require the use of expensive equipment like mass spectrometers.
Bio-Techne scientist Zhengliang Wu, Ph.D., and his team, are attempting to address this unmet need for new glycobiology research tools. In a series of publications, Dr. Wu and his colleagues describe new enzyme-based techniques that will allow researchers to study glycans using reagents and equipment found in almost any laboratory. The latest publication in Cell Chemical Biology describes a method to measure a unique sugar called O-GlcNAc, which is found attached to the amino acids serine and threonine of cellular proteins. The presence of O-GlcNAc on a protein can affect its biological activity, half-life, and immunogenicity. What makes protein glycosylation with O-GlcNAc especially interesting is its similarity to protein phosphorylation, a modification where phosphate is added to the same amino acids of proteins. Factors associated with the process of phosphorylation are widely studied as potential drug targets. By publishing these new techniques, Bio-Techne hopes to encourage more scientists to study glycobiology so that the link between glycosylation and disease can be better understood.
Dave Eansor, President of Bio-Techne's Protein Sciences Segment, commented, "There is a rapidly expanding interest in glycobiology, and a well-known lack of specific, easy-to-use research tools. Bio-Techne's innovative scientists are closing that gap and we look forward to helping advance this important area of biology."
Contact: Dave Eansor, President, Protein Sciences Segment, 612-379-2956
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