Cathepsin S Protein (recombinant mouse)

Activity: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVENval-WRK (Dnp)-NH2, AnaSpec, Catalog # 27114.The specific activity is >300 pmoles/min/µg.(Activation description: The enzyme achieves its activity under acidic pH) Protein Construction: Recombinant Mouse Cathepsin S is produced by our Mammalian expression system and the target gene encoding Val18-Ile340 is expressed with a 6His tag at the C-terminus. Sequence: Met 1-Ile 340. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 13&30 kDa. Protein function: Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. This protein is expressed by antigen presenting cells including macrophages, B-lymphocytes, dendritic cells and microglia. Moreover, cathepsin S is expressed in some epithelial cells. Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung. In addition, evidences indicated that cathepsin S generates A beta from amyloidogenic fragments of beta APP in the endosomal/lysosomal compartment, and is implicated in the pathogenesis of Alzheimer's disease (AD) and Down Syndrome (DS). Protein function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L. [The UniProt Consortium]