Applications
-
WB
-
IHC-P
REACTIVITY
-
Human
SPECIFICATIONS
Product Type
Mouse monoclonal primary
Product Name
Cathepsin D Monoclonal Antibody (EM1901-02)
Immunogen
Recombinant protein within human cathepsin d aa 1-432.
Host
Mouse
Positive Control
MCF-7, human liver tissue, human liver cancer tissue.
Conjugation
Unconjugated
Clonality
Monoclonal
Clone Number
13F3
PROPERTIES
Form
Liquid
Storage Condition
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
Storage Buffer
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Concentration
2 ug/ul
PURIFICATION
Protein affinity purified.
MOLECULAR WEIGHT
28/43/46 kDa
Isotype
IgG1
APPLICATION DILUTION
-
WB:1:10,000-1:50,000
-
IHC-P:1:50-1:200
TARGET
UNIPROT #
PROTEIN NAME
Cathepsin D
SYNONYMS
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
SEQUENCE SIMILARITIES
Belongs to the peptidase A1 family.
TISSUE SPECIFICITY
Expressed in the aorta extracellular space (at protein level). Expressed in liver (at protein level).
POST-TRANSLATIONAL MODIFICATION
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.
SUBCELLULAR LOCATION
Lysosome. Melanosome. Secreted, extracellular space.
FUNCTION
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.