||Recombinant Human Hemopexin-Like Domain of MMP1 (Interstitial collagenase, matrix metalloproteinase 1), cloned from human cDNA, was expressed inE. coli. The protein consists of the hemopexin-like domain of human MMP-1 (residues 274-470, swissprot accession P03956 ). MW = 23.2 kDa.
||Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP"s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes a secreted enzyme which breaks down the interstitial collagens, types I, II, and III. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.In addition, mechanical force may increase the expression of MMP1 in human periodontal ligament cells.
||> 95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight between 20 and 30 kDa.
||solution in 50mM Tris pH 7.2, 300mM NaCl, 0.1mM ZnCl2, 20mM CaCl2. The concentration is calculated from the absorbance at 280nm (e280 = 41495 M-1 cm-1).
||Under the above described conditions, the product has been concentrated up to 200μM without observing precipitation.