Cathepsin L2
Cathepsin U

Frozen liquid. In 800 mM NaCl, 25 mM sodium acetate, 0.8 M NaCl, pH 5.0. AVOID FREEZE/THAW CYCLES. Recombinant, human procathepsin V (amino acids 18-334) fused at the N-terminus to a CD33 signal sequence (amino acids 1-16) and at the C-terminus to a His•Tag^® sequence and expressed in NSO cells. Cat V is predominantly expressed in normal thymus, testis, and corneal epithelium. It is involved in the invariant chain degradation in thymic epithelial cells and its overexpression has been detected in myasthenia gravis. Abnormally wide spread expressions in mammary gland and colon have also been reported in breast and colonrectal carcinomas. Although it shows high amino acid identity with cathepsin L (Cat. No. 219382), these two cathepsins have very different tissue distribution and substrate specificity. As a result of glycosylation, this recombinant enzyme migrates ~40 kDa on SDS-PAGE under either reducing or non-reducing conditions. Requires activation prior to use. Specific activity: ≥300 units/µg. One unit is defined as the amount of enzyme that will cleave 1 pmol the fluorescent substrate Z-LR-AMC per min at 25°C, pH 5.5. Purity: ≥95% by SDS-PAGE. Contaminants: Endotoxins: ≤1.0 EU/µg Cathepsin V. EC 3.4.22.43.

Ref.: Tolosa, E., et al. 2003. J. Clin. Invest. 112, 517. Turk, V., et al. 2001. EMBO J. 20, 4629. Somoza, J.R., et al. 2000. Biochemistry 39, 12543. Bromme, D., et al. 1999. Biochemistry 38, 2377. Adachi, W., et al. 1998. Invest. Ophthalmol. Vis. Sci. 39, 1789. Santamaria, I., et al. 1998. Cancer Res. 58, 1624.