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 .
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
CTSC polyclonal antibody detects endogenous levels of CTSC protein.
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