Cathepsin C Antibodies
Cathepsin C, known also as dipeptidyl aminopeptidase I (DPPI), is a tetrameric lysosomal cysteine peptidase belonging to the papain family. Cathepsin C is involved in intracellular protein degradation and the processing of protein precursors, where it participates in cell growth, neuraminidase activation, and platelet factor XIII activation. Cathepsin C is largely related to other lysosomal cysteine proteinases, including cathepsin B, H and L. Enzymatically, Cathepsin C is capable of sequentially removing dipeptides from the amino terminus, and it requires halide ions, namely chloride ions, and thiols for complete enzymatic activity. Protein levels of Cathepsin C are detected in a variety of tissues, and it is most highly expressed in spleen, kidney, cytotoxic lymphocytes and myeloid cells, where it localizes to the secretory granule compartment. Cathepsin C is initially synthesized as a proenzyme that is rapidly processed to generate two distinct chains that function together as the mature form of the enzyme.
Cathepsin C; Cathepsin J; Dipeptidyl peptidase 1; Dipeptidyl peptidase 1 exclusion domain chain; Dipeptidyl peptidase 1 heavy chain; Dipeptidyl peptidase 1 light chain; Dipeptidyl peptidase I; Dipeptidyl peptidase I exclusion domain chain; Dipeptidyl peptidase I heavy chain; Dipeptidyl peptidase I light chain; Dipeptidyl transferase; dipeptidyl-peptidase; dipeptidyl-peptidase I; DPP-I