Cathepsin D Active Protein | CTSD active protein

Cathepsin D, Human (CatD, CLN10, CPSD, CTSD, Lysosomal Aspartyl Peptidase, MGC2311)

Cat. Num. AAA634930

• Gene Names: CTSD; CPSD; CLN10
• Purity: Purified; 95% by SDS-PAGE
• Synonyms: Cathepsin D; Human (CatD; CLN10; CPSD; CTSD; Lysosomal Aspartyl Peptidase; MGC2311); CTSD active protein

• Host: Human Liver
• Purity/Purification: Purified; 95% by SDS-PAGE
• Form/Format: Supplied as a lyophilized powder from 2mM sodium phosphate, pH 6.5. Reconstitution: Reconstitute with ~200ul sterile distilled water.

• Specific Activity: ~300u/mg
• Unit Definition: 1 unit is the amount of enzyme that digests hemoglobin-releasing peptides which are soluble in 10% TCA. The reaction is measured by an increase of an A280 of 1.0 per 60 minutes at 37 degree C. Substrate: Acid denatured hemoglobin (0.2% in reaction mixture). Buffer: 0.1M formate, pH 3.3.
• Preparation and Storage: Lyophilized powder may be stored at -20 degree C. Stable for 12 months at -20 degree C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for CTSD active protein

Cathepsins are localized primarily in lysosomes or endosomes, but translocated to the cytosol during apoptosis. The translocation allows these proteases to interact with caspases or other apoptosis signaling mechanisms. Studies show that cathepsins cleave certain caspases, and caspase inhibitors can inhibit cathepsin activity in vitro.

Cathepsin D is a normal lysosomal protease that is expressed in all cells. It is an aspartyl protease with a pH optimum in the range of 3-5, and contains two N-linked oligosaccharides. Cathepsin D is synthesized as an inactive 52kD pro-enzyme. Activation involves the proteolytic removal of the 43 amino acid profragment and an internal cleavage to generate the two-chain form made up of 34 and 14kD subunits.
Cathepsin D contains the mannose-6-phosphate lysosomal localization signal that targets the enzyme to the lysosomal compartment where it functions in the normal degradation of proteins. In certain tumor cells, Cathepsin D is abnormally processed and is secreted in its 52kD precursor form. Numerous clinical studies as well as in vitro evidence suggest that cathepsin D plays an important role in malignant transformation and may be a useful prognostic indicator for breast cancer.

Product Categories/Family for CTSD active protein

Molecular Biology; MB-Cathepsin

NCBI and Uniprot Product Information

• NCBI GI #: 4503143
• NCBI GeneID: 1509
• NCBI Accession #: NP_001900.1
• NCBI GenBank Nucleotide #: NM_001909.4
• UniProt Accession #: P07339; Q6IB57
• Molecular Weight: 44,552 Da
• NCBI Official Full Name: cathepsin D preproprotein
• NCBI Official Synonym Full Names: cathepsin D
• NCBI Official Symbol: CTSD
• NCBI Official Synonym Symbols: CPSD; CLN10
• NCBI Protein Information: cathepsin D; lysosomal aspartyl protease; lysosomal aspartyl peptidase; ceroid-lipofuscinosis, neuronal 10
• UniProt Protein Name: Cathepsin D
• Protein Family: Cathepsin
• UniProt Gene Name: CTSD
• UniProt Synonym Gene Names: CPSD
• UniProt Entry Name: CATD_HUMAN

NCBI Description

This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. [provided by RefSeq, Jul 2008]

Uniprot Description

CTSD: Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. Consists of a light chain and a heavy chain. Belongs to the peptidase A1 family.

Protein type: EC 3.4.23.5; Autophagy; Motility/polarity/chemotaxis; Protease

Chromosomal Location of Human Ortholog: 11p15.5

Cellular Component: extracellular matrix; extracellular space; lysosomal lumen; lysosome; extracellular region; melanosome

Molecular Function: protein binding; aspartic-type endopeptidase activity

Biological Process: collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; antigen processing and presentation of exogenous peptide antigen via MHC class II; proteolysis

Disease: Ceroid Lipofuscinosis, Neuronal, 10