Description
Cathepsin C/DPPI, also known as dipeptidyl peptidase I, is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. It catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if the amino group of the N-terminus is blocked. Also, It appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Defects in the Cathepsin C have been shown to be a cause of Papillon-Lefevre disease, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Also, It plays a key role in the activation of several degradative enzymes linked to tissue destruction in inflammatory diseases. Recombinant mouse Cathepsin C, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques