Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2. The specific activity is >200 pmol/min/μg, as measured under the described conditions.
Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.
Post-translational: The precursor is cleaved by a furin endopeptidase.
生物活性
Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2. The specific activity is >200 pmol/min/μg, as measured under the described conditions.
Lyophilized from 50mM Tris, 250mM NaCl, 5% Trehalose, pH8.0.
复溶
Reconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
长期储存-20~-80℃(1年);复溶后建议分装,避免反复冻融。
图片
Recombinant Human MMP-15/MT2-MMP Protein (rp165189) - SDS-PAGE 2 μg/lane of Recombinant Human MMP-15/MT2-MMP Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the band at 68 kDa under reducing conditions and 68 & 130 kDa under non-reducing conditions. MMP-15/MT2-MMP's auto-catalysis is an inherent characteristic of the matrix metalloproteinase (MMP) family. This property may lead to self-degradation or cleavage of contaminating proteins during purification, resulting in fragment bands.