Characterise antibody Fc interactions using SPR
With our in-house produced high quality Fcγ and FcRn receptors and two state-of-the-art Biacore 8Ks on site, we offer high throughput and high performance assays, to get the binding data you need while saving you time and money. Why select us?
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Better value
Our quality-controlled production yields receptors of high purity, quantity and function at a fraction of the cost of most commercially available equivalents.
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More accurate data
Inverse orientation means interference from non-specific binding of ‘sticky’ material is eliminated.
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Low test sample requirement
With Fc receptor proteins as the analyte, lower quantities of your precious test antibodies are required.
Assess binding dependencies by SPR
Differential affinity is key to maximising the therapeutic window of immune cell engagers. Have you considered how single occupation of an antibody binding domain may affect a 'cis' interaction? This is especially relevant to T cell engagers, where target antigen binding can influence the kinetics of the interaction of anti-CD3 arm with the T cell. Understanding binding dependencies is critical for the prediction of functional activity, and extends beyond immune cell engagers to all classes of bispecific and multispecific antibodies and even conventional monoclonals.
Our dependent binding assessments can be applied to T cell engagers, bispecifics and even to determine how the Fab-antigen interaction of an IgG1 molecule may affect the interaction of the Fc domain with Fc receptors. We have established a range of SPR assay designs to interrogate these dependencies. These can be applied across the drug discovery life cycle.
