Endoglycosidases useful for the analysis and evaluation of antibody drugs and ADCs (antibody-drug conjugates) including biosimilars.
GlycINATOR (EndoS2) is an endoglycosidase derived from Streptococcus pyogenes that hydrolyzes the glycan chains in the Fc region of IgG. This enzyme has been shown to remove all glycan structures (glycoforms) on IgG, including high-mannose, hybrid, complex, and bisecting type glycans (Sjögren et al. 2015). It deglycosylates human IgG (all subclasses) as well as IgG from many different animal species, including mice, rats, monkeys, sheep, goats, cows, and horses. However, its activity against glycans derived from alpha-1-acid glycoprotein has been reported to be limited (Sjögren et al. 2013). This enzyme is expressed and produced in Escherichia coli, contains a His tag, and has a molecular weight of 92 kDa. This enzyme is useful for reducing the complexity of antibody-based therapies and for studying fucose modifications and the occupancy of N-linked glycans. Rapid and mild reaction conditions minimize the risk of modifications during sample pretreatment (Sjögren et al. 2015).
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<Main Product Lineup> GlycINATOR Enzyme Lyophilized product. 2000 units. Immobilized GlycINATOR Spin column filling product. Since GlycINATOR is immobilized on agarose beads, it can highly prevent contamination from GlycINATOR and obtain the desired preparation. <Other Products> GlycINATOR LE (Low Endotoxin) ● Genovis actively holds web meetings and seminars. Please feel free to contact us as we can adjust according to your requests.
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Analysis of Afucosylation levels in antibodies Reduction of complexity in antibody samples Study of antibodies without fucose modification
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Rohmatsu Trading Co., Ltd. engages in the procurement, research, and contracting of overseas chemical products, as well as providing information on them. From the top management to all employees, we unite as one, always keeping five keywords in mind, continuously striving for creativity and ingenuity, and serving the market to contribute to society.