Lucentis VEGF Binding Assays

At BioOutsource, the combination of experience in the inception, optimization, and qualification of binding assays for various monoclonal antibody therapeutics is coupled with a pioneering approach to bioassay development.

Lucentis (ranibizumab) mediates its activity through a high-affinity interaction with VEGF to mediate a number of different outcomes; therefore, VEGF binding by Lucentis, (as with all antibody-antigen interactions), represents one of the key quality attributes of the Lucentis (ranibizumab) molecule.  Protein-protein interaction assays using a diverse range of techniques can be used to evaluate the interaction between the epitope recognition sites of Lucentis (ranibizumab) and various isoforms of the VEGF target protein.

The affinity of Lucentis (ranibizumab) material for its target molecule is a key defining characteristic which drives the need for subsequent interrogation of biological activity.  BioOutsource offers the following assays to characterize the interaction between Lucentis (ranibizumab) and VEGF isoforms to provide data from orthogonal methods for clone selection, process development and similarity studies:

Lucentis VEGF Binding ELISA

BioOutsource offers Lucentis VEGF binding assays using a competition ELISA format to report the relative binding of biosimilar and innovator Lucentis material to a number of VEGF isoforms as a percentage of a designated reference lot, with comprehensive parallelism assessments.

Lucentis VEGF Binding by SPR

BioOutsource has expanded on the Lucentis VEGF binding ELISA concept and offers an enhanced VEGF binding assay that significantly increases the understanding of the Lucentis VEGF binding during comparability studies.

We are pleased to offer analysis of the Lucentis VEGF binding interaction by surface plasmon resonance (SPR).  By leveraging the exquisite sensitivity offered by Biacore T200 instruments we report full kinetic data for this high affinity interaction, including Affinity Constants (KD), with the association or “on” rate (Ka) and dissociation rate (Kd) or “off” rate. The data is also evaluated to generate relative binding and parallelism assessments.