Cleaved-Cathepsin O (L108) polyclonal antibody

The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. The cysteine protease class comprises cathepsins B, L, H, K, S, and O. The aspartyl protease class is composed of cathepsins D and E. Cathepsin G is in the serine protease class. Most cathepsins are lysosomal and each is involved in cellular metabolism, participating in various events such as peptide biosynthesis and protein degradation. Cathepsin O maintains the structural features characteristic of other cysteine proteinases including the active site cysteine residue that is involved in covalent intermediate formation during peptide hydrolysis. Cathepsin O is an endoproteinase that may be involved in extracellular matrix degradation. Cathepsin O is abundantly expressed in the ovary, kidney and placenta with lower levels found in thymus and skeletal muscle.