Recombinant Prokaryotic Lectins
Functional analysis of sugar chains
Lectins are proteins capable of recognizing and binding specific glycan structures displayed on biomolecules. By interacting with glycans and glycosylated biomolecules, they are able to mediate a broad range of biological processes. Since the discovery of lectins, their applications have been found to be widespread, diverse and valuable for the detection, analysis and isolation of intact glycosylated biomolecules. This is a large contrast to traditional glycoanalytical methods, which are both complex and time-consuming even with highly trained researcher.
Enhancing the Affinity of RPLs
Altering the Specificity of RPLs
Lectin Engineering: Both RPL-Gal2 (left) and RPL-Gal1 (right) were derived from the alpha-galactophilic lectin RPL-aGal through the use of site specific mutagenesis. RPL-Gal2 exhibits significantly enhanced affinity for terminal alpha-linked galactose than either the parental RPL-aGal or the comparable plant lectin GSL-1 (approx 5 fold). RPL-Gal1 exhibits high affinity binding to terminal beta-1,4-linked galactose, to which the parental RPL-aGal doesn't bind, significantly greater than that of the comparable plant lectin ECL (approx 10 fold).