Cathepsin L1 human

Cathepsin L (CTSL1) also known as major excreted protein (MEP), is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains linked by disulfide bonds. CTSL1 is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as α-1 protease inhibitor, a major controlling element of neutrophil elastase activity. MEP has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. CTSL1 is important for the overall degradation of proteins in lysosomes. The specificity of MEP is close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z - Arg – Arg – NHMec, and no peptidyl - dipeptidase activity. Human Cathepsin L activity is greatest under mildly acidic conditions, from pH 4.5 ­ 6.5. The stability of the enzyme decreases at higher pH values.

DTT-reduced. Protein migrates due to glycosylation, corresponding to the propeptide and the mature form respectively. Thr 18 and Ala 114 is the predicted N-terminal.

Lyophilized from 0.22 μm filtered solution in 50 mM Sodium Acetate, pH 5.0 with 100 mM NaCl. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.