Cathepsin B Active Protein | CTSB active protein

Cathepsin B

Cat. Num. AAA634648

• Purity: Highly Purified; 95% by SDS-PAGE
• Synonyms: Cathepsin B; CTSB active protein

• Host: Human liver
• Purity/Purification: Highly Purified; 95% by SDS-PAGE
• Form/Format: Supplied as a liquid in 50mM sodium acetate, pH 5.0, with 1mM EDTA.

• Activity: 200 Units/mg protein using Z-Arg-Arg-beta-NA as a substrate. One unit is defined as the amount of enzyme that hydrolyzes one umole of 2-naphtylamine per minute at 40 degree C, pH 6.0.
• Preparation and Storage: For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.

Related Product Information for CTSB 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.

Product Categories/Family for CTSB active protein

Molecular Biology; MB-Cathepsin

NCBI and Uniprot Product Information

• NCBI GI #: 27806671
• NCBI GeneID: 281105
• NCBI Accession #: NP_776456.1
• NCBI GenBank Nucleotide #: NM_174031.2
• UniProt Accession #: P07688; Q3ZC03
• Molecular Weight: 36,661 Da
• NCBI Official Full Name: cathepsin B
• NCBI Official Synonym Full Names: cathepsin B<
• NCBI Official Symbol: CTSB
• NCBI Protein Information: cathepsin B; BCSB
• UniProt Protein Name: Cathepsin B
• Protein Family: Cathepsin
• UniProt Gene Name: CTSB
• UniProt Entry Name: CATB_BOVIN

Uniprot Description

Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Catalytic activity: Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.

Subunit structure: Interacts with SRPX2

By similarity. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Subcellular location: Lysosome. Melanosome

By similarity. Secreted › extracellular space

By similarity.

Sequence similarities: Belongs to the peptidase C1 family.