Cathepsin D Recombinant Mouse Monoclonal Antibody [13F3-R]

The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. These products include the cathepsin D light and heavy chains, which heterodimerize to form the mature enzyme. This enzyme exhibits pepsin-like activity and plays a role in protein turnover and in the proteolytic activation of hormones and growth factors. 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. Cathepsins may also cleave some protein precursors, thereby releasing regulatory peptides. The promoter region of the cathepsin D gene contains five Sp1 binding sites and four AP-2 binding sites. Mutations in this gene play a causal role in neuronal ceroid lipofuscinosis-10 and may be involved in the pathogenesis of several other diseases, including breast cancer and possibly Alzheimer's disease.