MMP1 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin and so on. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain. The activity of recombinant pig MMP1 is measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rpMMP1 is diluted to 50 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 °C for 2 hours. The activated rpMMP-1 is diluted to 1 ug/mL in assay buffer. Loading into a black well plate 50 µL of 1 ug/mL rpMMP-1 and start the reaction by adding 50 µL of 20 µM substrate, with a substrate blank containing 50 µL assay buffer, 50 µL substrate, and no rpMMP-1. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant pig MMP1 is > 10 pmol/min/µg.