Mouse anti-MT1-MMP/MMP14 monoclonal antibody, clone LEM-2/15 targets MT1-MMP / MMP14 V-B-loop exosite. The supplied structural record is associated with PDB 4OUU; 4P3C; 4P3D; 4QXU.
Recognizes the exposed MT1-MMP/MMP14 V-B-loop exosite rather than the catalytic zinc center. The isolated peptide complexes directly define the V-B-loop interaction; binding perturbs productive substrate access without occupying the catalytic center. Noncompetitive inhibitor of MT1-MMP/MMP14; reported to inhibit degradation of physiological collagen and gelatin substrates. The intact enzyme is described as a nanomolar-affinity target, but no exact equilibrium Kd was provided in the supplied material. 4OUU is unliganded; 4P3C/4P3D and 4QXU contain isolated V-B-loop peptides rather than the complete catalytic domain. Peptide complexes alone do not establish global catalytic-domain rearrangement, and whole-enzyme mechanism also depends on enzyme assays.
Product-specific preparation, formulation, size, storage, and shipping conditions were not specified in the supplied source.
Summary
Specifications
Antibody Isotype
IgG
Clone
LEM-2/15
Conjugate
Unconjugated
Applications
Application Notes
Inhibition, IA, ELISA This antibody acts as a noncompetitive inhibitor of MT1-MMP/MMP14 and inhibits degradation of physiological collagen and gelatin substrates. It is used in selective MT1-MMP inhibition, metalloprotease exosite research, and ECM degradation studies. Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded
General Notes
Noncompetitive inhibitor of MT1-MMP/MMP14; reported to inhibit degradation of physiological collagen and gelatin substrates. The intact enzyme is described as a nanomolar-affinity target, but no exact equilibrium Kd was provided in the supplied material. 4OUU is unliganded; 4P3C/4P3D and 4QXU contain isolated V-B-loop peptides rather than the complete catalytic domain. Peptide complexes alone do not establish global catalytic-domain rearrangement, and whole-enzyme mechanism also depends on enzyme assays.
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