Enzyme Commission Number
EC 3.4.18.1
Product Overview
High-quality enzyme products.
Well-established quality management system.
Reaction
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
Function
Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13.
Other name
cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B
Production Methods
Fermentation
Package
on customer request
Applications
Research Use
Storage
Should be stored in a dry and cool place, avoiding high temperature.
Appearance / Form
powder or liquid
Odor
Normal microbial fermentation odour.
WARNINGS
Keep sealed after use every time to avoid microbial infections and inactivation of enzymes until its finish.
Description
Microbial enzymes have been used in a large number of fields, such as chemical, agricultural and biopharmaceutical industries. Our enzyme production services are based on bacteria, fungi, and yeast, from strain selection, optimization, and process development to scale-up production.
