Altering the Specificity of RPLs

Enhancing the Affinity of RPLs

Lectin Engineering - Enhanced & Tailored Glycan Recognition

Superior Perfomance

Consistent High Quality & Purity

High Level Expression in Escherichia coli: Because of their origin prokaryotic lectins are more amenable to recombinant expression, to high levels, in E. coli

RPLs - Enhanced Glycoselective Tools for the Life Sciences

​​High Sensitivity:  In standard ELLA formats RPLs enable significantly greater sensitivity of detection at lower lectin concentrations than that required for plant lectins (panels below).

​High Affinity:  RPLs exhibit greater selectivity and higher affinity for glycosylated targets than comparable plant and eukaryotic lectins (panels below).

Recombinant expression and selective affinity purification of RPLs results in the production of products of consistent high quality, purity and performance. This is in contrast to plant lectins for which variation in performance (from batch to batch and from one supplier to another) has traditionally been reported. 


Simple & Scalable Production

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).






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RPLs offer many advantages over traditional plant and eukaryotic lectins. The also offer many advantages over current glycoanalytical and chromatographic methodologies that are not glycoselective or require prior release of glycans which results in the sample destruction.

Recombinant production methods present opportunities to manipulate RPL glycan binding properties through the use of site specific mutagenesis strategies. Lectins can be engineered to enhance their affinity for a given glycan moiety (below left) or to alter their specificity for alternative glycan moieties (below right). This can allow RPL properties to be tailored for specific targets or to enhance their performance for specific applications.


High Capacity Affinity Purification: RPLs are expressed with genetically incorporated poly-histidine tags which enables simple one step and high capacity purification of products via immobilized metal affinity chromatography (IMAC).

Recombinant Prokaryotic Lectins (RPLs) are superior glycoselective biaffinity molecules that enable simple, fast and efficient detection, analysis and isolation of intact glycosylated biomolecules.

​Readily ​Scalable Production: RPLs expression is readily scalable using Stirred Tank Reactor (STR) systems. This combined with the high capacity and scalability of IMAC purification enables cost effective production of RPLs in sufficient quantities required for large scale applications in the separation and purification of glycosylated biomolecules.

High Stability & Robustness: RPLs exhibit excellent stablity enabling RPL bioaffinity matrices to be reused many times. Because of their prokaryotic origins RPLs lack the presence of disulphide bonds. This allows RPLs to be used in the presence of reducing agents for applications under denaturing conditions.