Anti-Human GPVI Recombinant Antibody scFv Fragment (1C3) (CAT#: TAB-003CT-S(P))

Figure 1 The effect of mutations on the activity of D1D2.

Epitope-mapping by ELISA. Wild-type D1D2 (wt) or the two point mutants (I148A, Y134A) were captured via the calmodulin tag to wells coated with BSA-N9A. The wells were incubated with scFv 1C3 (10 μg/ml), and then bound scFv was detected by 9E10-HRP.

O'Connor, M. N., Smethurst, P. A., Davies, L. W., Joutsi-Korhonen, L., Onley, D. J., Herr, A. B., ... & Ouwehand, W. H. (2006). Selective blockade of glycoprotein VI clustering on collagen helices. Journal of Biological Chemistry, 281(44), 33505-33510.

Figure 2 The effect of monomeric 1C3 on binding of D1D2 to immobilized (GPO)x peptides.

D1D2 (10 μg/ml) was preincubated with increasing concentrations of freshly purified monomeric 1C3 scFv for 2 h. D1D2/1C3 was added to peptides GPO2 (circles), GPO4 (triangles), GPO6 (squares), or the control peptide GPP10 that had been immobilized on a maxisorp plate and incubated for 20 min. Bound CaM-tagged D1D2 was detected with N9A-HRP. Nonspecific binding of D1D2 to GPP10 was subtracted from each data point, and values are the mean ± S.D. of three determinations.

O'Connor, M. N., Smethurst, P. A., Davies, L. W., Joutsi-Korhonen, L., Onley, D. J., Herr, A. B., ... & Ouwehand, W. H. (2006). Selective blockade of glycoprotein VI clustering on collagen helices. Journal of Biological Chemistry, 281(44), 33505-33510.