Recombinant Human Antibody (A11) is capable of binding to MT-SP1, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-MT-SP1 mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-MT-SP1 proteins mAb and CL of human light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. This antibody was identified with a 720 pM inhibition constant and high specificity for matriptase over other trypsin-fold serine proteases.
Figure 1 Antibodies are specific for active MT-SP1.
SPR binding curves of MT-SP1 (black) and the zymogen-like mutant R15A (gray) to the A11 Fab show robust binding to active enzyme and a lack of binding to the zymogen, indicating that the inhibitor is specific for the active form of the enzyme. Binding assays with enzyme concentrations up to 1 μmol/L showed similar results (not shown). RU, resonance unit.
Darragh, M. R., Schneider, E. L., Lou, J., Phojanakong, P. J., Farady, C. J., Marks, J. D., ... & Craik, C. S. (2010). Tumor detection by imaging proteolytic activity. Cancer research, 0008-5472.
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