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Reconstituted by adding 0.5 mL sterile distilled water, spun down to remove insoluble particles, divided into small aliquots, frozen and stored at or below -20°C.
Cross-reactivities against enzymes of other sources may occur but have not been determined.
Prior to use, an aliquot is thawed slowly at ambient temperature, spun down again and used to prepare working dilutions by adding sterile phosphate buffered saline (PBS, pH 7.2). Repeated thawing and freezing should be avoided. Working dilutions should be stored at 4°C, not refrozen, and preferably used t he same day. If a slight precipitation occurs upon storage, this should be removed by centrifugation. It will not affect the performance of the product.
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: Cathepsin C; Cathepsin J; Dipeptidyl peptidase 1; Dipeptidyl peptidase I; Dipeptidyl transferase; dipeptidyl-peptidase; DPP-I; DPPI
基因别名: CTSC
UniProt ID: (Bovine) Q3ZCJ8
Entrez Gene ID: (Bovine) 352958