CTSZ / CTSX / Cathepsin Z Protein (His tag) (recombinant mouse)

Activity: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK(Dnp)-OH (R&D Systems, Catalog # ES005). The specific activity is >1,200 pmoles/min/µg. Protein Construction: A DNA sequence encoding the mouse CTSZ (NP_071720.1) precursor (Met 1-Val 306) was expressed with a polyhistidine tag at the C-terminus. Sequence: Met 1-Val 306. Fusion tag: C-His Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 38 kDa. Protein function: Cathepsin Z (CTSZ), also known as Cathepsin X or CATX, belongs to the C1 family of lysosomal cysteine proteases. Its gene structure and activity properties show several unique features that distinguish it clearly from other human cysteine proteases. It has a very short pro-region that shows no similarity to those of other cathepsins and a three-residue insertion motif that forms a characteristic 'mini loop'. Cathepsin Z exhibits mono- and di-peptidase activity at its C-terminus, and in contrast to cathepsin B, it does not act as an endopeptidase. It is restricted to the cells of theimmune system, predominantly monocytes, macrophages and dendritic cells. Cathepsin Z is widely expressed in human tissues, suggesting that this enzyme could be involved in the normal intracellular protein degradation taking place in all cell types. It is capable to cleave regulatory motifs at C-terminus affecting the function of targeted molecules. Cathepsin X may regulate also the maturation of dendritic cells, a proc Protein function: Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity. [The UniProt Consortium]