Mouse monoclonal primary
Cathepsin D Monoclonal Antibody (EM1901-02)
Recombinant protein within human cathepsin d aa 1-432.
MCF-7, human liver tissue, human liver cancer tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein affinity purified.
CatD antibody; CATD_HUMAN antibody; Cathepsin D antibody; Cathepsin D heavy chain antibody; CD antibody; Ceroid lipofuscinosis neuronal 10 antibody; CLN10 antibody; CPSD antibody; ctsd antibody; Epididymis secretory sperm binding protein Li 130P antibody; HEL S 130P antibody; Lysosomal aspartyl peptidase antibody; Lysosomal aspartyl protease antibody; MGC2311 antibody
Belongs to the peptidase A1 family.
Expressed in the aorta extracellular space (at protein level). Expressed in liver (at protein level).
N- and O-glycosylated.; Undergoes proteolytic cleavage and activation by ADAM30.; As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified. An additional form starting at Ala-168 has also been identified.
Lysosome. Melanosome. Secreted, extracellular space.
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.