Glycans play diverse roles in the biological properties of glycoproteins and changes in glycosylation can dramatically alter their function and activity. Determining the glycosylation of proteins is typically done using mass spectrometry or chromatography, which can be difficult and time consuming. As such, other alternatives, such as lectin microarrays, have been developed.
Lectenz Bio offers GlycoSenseTM, a multiplex bead-based glycan analysis kit, which excels where MS is neither needed nor practical. Yielding near real-time results, this kit can be used with a basic flow cytometer and allows for monitoring of glycosylation during protein expression and glyco enzyme reactions.
The terminal glycosylation on glycoproteins, such as biologics or antibodies, can be monitored during protein production.
Fetuin treated with sialidase for one hour, followed by galactosidase for two hours. The data was BSA subtracted and normalized to the highest signal for each bead. As expected, sialic acid signals decrease concomitantly with the increase in galactose signal. With the addition of galactosidase at 60 minutes, galactose signal decreases due to cleavage of galactose, and GlcNAc signal increases simultaneously from newly exposed GlcNAc.