Cathepsins are involved in numerous normal and pathological processes. Cathepsin A is a member of the serine carboxypeptidase family. It is a multifunctional enzyme that possesses deaminidase and esterase activities at neutral pH and carboxypeptidase activity at acidic pH. Also known as a protective protein, its association with beta-galactosidase (beta-gal) and neuraminidase is essential for beta-gal stability and neuraminidase activation in lysosomes. Inherited cathepsin A deficiency causes the lysosomal storage disorder galactosialidosis. DPPI (cathepsin C) is a cysteine protease that sequentially removes dipeptides from the free N-termini of proteins and peptides. DPPI plays a role in lysosomal degradation. It also functions as a key enzyme in the activation of granule serine proteases in cytotoxic T lymphocytes and natural killer cells (granzymes A and B), mast cells (tryptase and chymase), and neutrophils (cathepsin G and elastase) by removing their N-terminal activation dipeptides. The lysosomal aspartic protease, cathepsin D, is essential for proteolysis of proteins regulating cell growth and tissue homeostasis. Cathepsin D is involved in breast and prostate cancer. Cathepsin X (also known as cathepsin Z and P) is a cysteine protease in the papain family. It is ubiquitously expressed in human tissues and conserved in many species. The nematode enzyme is apparently involved in molting of third stage larvae.
|Recombinant Mouse Cathepsin D||Recombinant Mouse (DPPI) Dipeptidyl-peptidase I/Cathepsin C|
Catalog: # 1029-AS-010
|Catalog: # 1034-CY-010
Source: NS0 cells
Size: 10 µg
Activity:Determined by cleavage of a
fluorescent peptide substrate (G-R-AMC) as measured by fluorescence. The specific activity, measured with 10 µM G-R-AMC and 10 ng of activated enzyme in 100 µL of 25 mM MES, 50 mM NaCl, 5 mM DTT, pH 6.0, at 24° C, is > 10,000 pmoles/min/µg.