​​

  Introduction      |       Products       |      Applications       |       Partnering       |       Events    

RPLs - Enhanced Glycoselective Tools for the Glycosciences

RPLs offer many advantages over traditional plant derived lectins exhibiting greater selectivity and higher affinity for specific glycan targets. RPLs can be used in a wide range of biochemical assays and binding can be detected without the need for prior in vitro labelling (e.g. biotinylation) by using commercially available conjugated antibodies directed against the genetically incorporated poly-histidine tags. Recombinant production ensures high quality products with more consistent and reliable performance which is of particular importance for diagnostic applications. RPLs enable the generation of more efficient, sensitive and high-throughput glycoanalytical platforms, and highly efficient glycoselective bioaffinity matrices, to  give scientists the tools they need to unlock the secrets of the glycome.

Changes can also occur in the glycans displayed on cell surfaces and biomolecules as a result of changes in the physiological status of cells. These changes can result in, or simply be indicative of, the onset of a disease state including many types of cancer and autoimmune disorders. Tools enabling the detection of such changes in glycosylation can be used for the identification of novel glycan based biomarkers and present opportunities for new diagnostic approaches.

Many glycoanalytical methods require the prior release of glycans from a sample followed by their separation and identification by HPLC and MS based approaches. To perform such analysis there can be a pre-requiste need to isolate the biomolecules of interest from complex biological samples in which they are often only present at low concentrations. The release of glycans can from biomolecules can also result in the loss of biologically significant information including the location and distribution of glycans on a biomolecule or cell surface, factors can play a significant role in dictating biomolecular interactions that mediate complex biological processes. The ability of lectins to recognize and bind to glycans in situ has therefore made them valuable tools in the Glycoscience field for the detection, analysis and selective purification of intact glycosylated biomolecules. 

Glycoanalysis of Intact Biomolecules & Cells

Biomarker Discovery & Diagnostics

The ability to detect, isolate and analyse glycosylated molecules is therefore essential for our ability to characterise this important class of biological molecules and to decipher the underlying molecular mechanisms of complex biological processes.

The nature of the glycans displayed on cell surfaces and biomolecules can be organism and cell type specific. Tools enabling the detection and analysis of glycans in situ can therefore be used for cell typing including the identification and classification of microorganisms and other infectious agents. 

As the interface between a cell and its environment it is not surprising that cell surface glycans mediate a vast array of biological processes, often through interaction with carbohydrate binding proteins called Lectins. They play  keys roles in processes like cell signaling, migration and in the orchestration of the immune system. They also mediate interactions with many infectious agents such as prions, viruses and microorganisms. The glycans present on biomolecules can also have a significant impact on their physiochemical properties and biological activity. 


Glycosylation is one of the most abundant and biologically significant post-translational modifications to occur in cells. Cell surfaces, both prokaryotic and eukaryotic, are covered in a dense layer of complex oligosaccharide structures that are attached to proteins and lipids. This layer is called the “glycocalyx”. 



Back       Menu       Next

Research & Diagnostics