Recombinant Human Antibody (AbD1556) is capable of binding to BMPR-IA, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-BMPR-IA mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-BMPR-IA proteins mAb and CL of human kappa light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition.
Figure 1 Functional epitopes of AbD1156, AbD1564 and BMP-2.
Mutational analysis of the BMPR-IA binding epitope and in vitro interaction analysis shows that the contribution of residues within the epitope to the binding energy correlate for binding to AbD1556 and BMP-2, whereasthe two Fab AbD1556 and AbD1564 clearly bind to BMPR-IA via a different mechanism.
Harth, S., Kotzsch, A., Hu, J., Sebald, W., & Mueller, T. D. (2010). A selection fit mechanism in BMP receptor IA as a possible source for BMP ligand-receptor promiscuity. PloS one, 5(9).
Figure 2 SPR analysis of BMPR-IA binding to BMP-2 and Fab proteins.
Sensorgram of the interaction of wild type BMPR-IA (red) and the BMPR-IA variant Q86A (blue) with AbD1556.
Harth, S., Kotzsch, A., Hu, J., Sebald, W., & Mueller, T. D. (2010). A selection fit mechanism in BMP receptor IA as a possible source for BMP ligand-receptor promiscuity. PloS one, 5(9).
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• Increased sensitivity
• Confirmed specificity
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