Sentence examples for binding to this mAb from inspiring English sources

The short V3-CTB presenting a V3 fragment in the conformation observed in the complex with the 447-52D Fab, exhibited high-affinity binding to this mAb.

The mAb-competitor mixtures were then added to wells with plastic-adsorbed Candida β-glucan (GG-Zym) and residual mAb binding to this latter was measured as described above.

The protein is affinity purified from this fraction by binding to anti-Flag mAb (M2) beads and recovered by elution with Flag peptide.

We developed a convenient assay for the detection of this particular mutation based on analysis of the plasma ACE binding to mAb 1B3 (directed to the C-terminal part of soluble ACE) and binding to mAb 9B9 (on the N-terminal domain of ACE).

Peptides corresponding to these regions were designed and evaluated for binding to mAb 69-126-3 by ELISandnd BioLayer Interferometry (BLI).

We observed accumulation of both measured glycation products (CEL and antigen binding to mAb 103-E3) in sera of RA patients.

To begin to identify a smaller fragment in the carboxyl region of EBNA-1 that contains the epitope recognized by 3D4, we examined the binding of this MAb to three truncated carboxyl fragments; EBNA452 641, EBNA459 619, and EBNA459 607 (Figure 7A).

Furthermore, preincubation of gp120 with murine anti-gp120 sera, elicited in the same strain of mice, up to saturating concentrations does not block the binding of biotinylated 426 MCP MAb (11A8), whereas the binding of this MAb is inhibited by antisera elicited by MCPs derived from this epitope (Figure 4A).

All VLPs containing G106/L107 substitutions exhibited reduced binding by this MAb, as did E311R VLPs.

Although fusion peptide substitutions did not alter the binding of this MAb, just as with MAb 5-1 all mutant VLPs containing combinations of E311 substitutions exhibited significant reductions in MAb 20 binding.

This study did not identify any substitutions in DENV-2 VLPs that disrupted the binding of this MAb.