Anti-LPA Recombinant Antibody Fab Fragment (LT3015 [B7(LT3000, Lpathomab)]) (CAT#: TAB-0340CL-F(E))

Figure 1 LPA binding affinity measured as in Figure for native LT3015 (WT) and three LT3015 single point mutations.

Fleming, J. K., Wojciak, J. M., Campbell, M. A., & Huxford, T. (2011). Biochemical and structural characterization of lysophosphatidic Acid binding by a humanized monoclonal antibody. Journal of molecular biology, 408(3), 462-476.

Figure 2 Site-directed mutagenesis and LPA binding assays of LT3015.

In comparison to native LT3015 (WT), the introduction of mutations in the LT3015 heavy chain (AsnH52Tyr/SerH52Tyr) or light chain (AnsL30Arg) does not significantly increase LPA affinity. However, their combination (AsnH52Tyr/SerH54Tyr/AsnL30Arg) results in a modified version of the antibody with increased LPA binding affinity.

Fleming, J. K., Wojciak, J. M., Campbell, M. A., & Huxford, T. (2011). Biochemical and structural characterization of lysophosphatidic Acid binding by a humanized monoclonal antibody. Journal of molecular biology, 408(3), 462-476.

Figure 3 is a plot of data for neuron-forming neurospheres in the absence or presence of LPA (1 μM) and/or anti-LPA mAbs (1 mg/ml) for 3 days.