Invitrogen™ Cathepsin C Polyclonal Antibody

Description

Immunogen sequence: SQEKYSNRLYK YDHNFVKAIN AIQKSWTATT YMEYETLTLG DMIRRSGGHS RKIPRPKPAP LT Highest antigen sequence identity to the following orthologs - mouse 70%, rat 71%.

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.