Cathepsin L1 HC (T288) 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 L (also designated major excreted protein, MEP or CATL) is a member of the peptidase C1 family and has been identified as a protein that is most closely related to cathepsin H. Cathepsin L is a lysosomal cysteine proteinase that mediates intracellular protein catabolism for collagen, elastin and α-1 protease inhibitor. Cathepsin L is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene. Transformed mouse fibroblasts stimulated by growth factors or tumor promoters secrete a form of cathepsin L.