Lectenz® is able to detect important glycan modifications independent of the sialic acid linkage (e.g.: α2,3 or α2,6 or α2,8), and shows no measurable affinity for related non-sialylated glycans. Such a reagent currently does not exist and would greatly assist in the development and detection of glycan-based disease markers, by enabling affinity enrichment of a sample in the glycopeptides or glycoproteins of interest.
Lectenz® innovate in two distinct ways:
The key innovations of Lectenz® reagents over existing glycomics reagents are:
Tunable affinities and binding kinetics (essential for applications in an affinity matrix)
Pre-defined, and potentially tunable, specificities – depending on the ligand employed in the directed
Evolution strategy and on the location of the mutagenesis sites
A platform technology that could be applied to a vast number of carbohydrate-processing enzymes
Including glycosyl hydrolases, transferases, lyases, esterases, etc...
What Makes Us Different
Advantage of our engineered Lectenz®: