Description_x000D_ Application_x000D_ Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels._x000D_ The enzyme from Sigma has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions._x000D_ Packaging_x000D_ 10, 25, 100 units in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators._x000D_ Caution_x000D_ Unstable. Keep frozen._x000D_ Unit Definition_x000D_ One unit will produce 1 μmole of Gly-Phe-NHOH from Gly-Phe-NH2 and hydroxylamine per min at pH 6.8 at 37 °C using DL-phenylalanine hydroxamic acid as the standard. In addition to its hydrolytic properties, cathepsin C catalyzes the polymerization of dipeptide amides._x000D_ Physical form_x000D_ Lyophilized from a 1 M sodium chloride solution.