Sentence examples for binding to different epitopes from inspiring English sources

Few studies have examined the clinical or pre-clinical effects of mAb binding to different epitopes of the same receptor.

Moreover, it has been shown that two different therapeutic antibodies, Gevokizumab and Canakinumab, activate two distinct pathways by binding to different epitopes of IL-1β (Blech et al., 2012).

To examine whether the differential effects of these IgG may be explained by their binding to different epitopes of the FXa active site, we compared the effects of APS-IgG, SLE-IgG and a 50/50 mix of these upon FXa activity to examine whether an appreciable increase in ability to inhibit FXa activity would be observed with the mixed APS/SLE-IgG samples.

To assess whether APS and SLE/APS- IgG may be binding to different epitopes on the active site of FXa, we selected different APS (n = 5) and SLE/APS- (n = 5) IgG on the basis of similar FXa binding and examined their individual and combined effects (at a final concentration of 200 μg/ml) upon FXa enzymatic activity.

We hypothesised that if APS and SLE/APS- IgG inhibited FXa on their own but were binding to different epitopes on the active site of FXa then an appreciable increase in inhibition of FXa activity would be observed with the mixed APS/SLE IgG preparations compared with individual APS or SLE samples.

In this study six HER2/neu-specific DARPins exhibiting different affinities and binding to different HER2/neu epitopes were applied as targeting domains.

Since it is known that anti-MUC1 aptamers [87] and antibodies binding to different MUC1 epitopes will be internalised [55], [88], [89], [50], [51], the internalisation of huHMFG1 and HT186-D11 wanalysedsed using MCF-7 cells.

Stringent criteria concerning the neutralizing activity, binding specificities to different epitopes, immunoglobulin isotype, and history of hybridomas were used to evaluate the suitability of several murine mAbs.

To quantify the differences in affinities, we compared binding to three different epitopes that all form part of a high-mannose oligosaccharide.

Furthermore, bi-paratopic BsAb, by simultaneously binding to two different epitopes on the same target molecule, could even potentially acquire new function that could not be achieved with the parent antibodies when used alone or in combination [56].

Using recombinant Fab (rFab) fragments derived from GAD65-specific monoclonal antibodies that bind to different conformational epitopes and parts of the protein [34], we performed competitive GAD65 binding assays.