Human Cathepsin L / CTSL1 Protein, His Tag (active enzyme)

Protein

Dry ice

37.8 kDa

Cathepsin L (CTSL1) is 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 alpha-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

Cathepsin L

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 37.8 kDa. The protein migrates as 31-33 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

50 mM NaAc, 0.5 M NaCl, pH4.5

glycerol