- Catalog number
- PKSH031883
- Size / count
- 50 µg
- Dry ice
- No
- Hazardous
- No
- Discontinued
- No
- Background
- Cathepsin V (CTSV), also known as Cathepsin L2, CTSL2, and CATL2, is a member of the peptidase C1 family. It is predominantly expressed in the thymus and testis. Cathepsin V is also expressed in corneal epithelium, and to a lesser extent in conjuctival epithelium and skin. It is a lysosomal cysteine proteinase that may play an important role in corneal physiology. It has about 75% protein sequence identity to murine cathepsin L. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. Cathepsin V has been recently described as highly homologous to Cathepsin L and exclusively expressed in human thymus and testis. Cathepsin V is the dominant cysteine protease in cortical human thymic epithelial cells, while Cathepsin L and Cathepsin S seem to be restricted to dendritic and macrophage-like cells. Active Cathepsin V in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant Cathepsin V was capable of converting Ii into CLIP efficiently, suggesting that it is the protease that controls the generation of alphabeta-CLIP complexes in the human thymus. Cathepsin V is the third elastolytic cysteine protease which exhibits the most potent elastase activity yet described among human proteases and that it is present in atherosclerotic plaque specimens. Cathepsin L2 may play a specialized role in the thymus and testis. Expression analysis of cathepsin L2 in human tumors revealed a widespread expression in colorectal and breast carcinomas but not in normal colon or mammary gland or in peritumoral tissues.
- Synonyms
- CATL2; CTSL2; CTSU; CTSV; Cathepsin L2; Cathepsin U; Cathepsin V
- UniProt
- O60911
- Accession Number
- NP_001324.2
- Expression System
- HEK293 Cells
- Tag
- C-His
- Sequence
- Met 1-Val 334
- Applications
- Enzyme
- Field of Research
- Signal Transduction
- Endotoxin
- < 1.0 EU per μg of the protein as determined by the LAL method.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Bioactivity
- Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC, (R&D Systems, Catalog # ES008) . The specific activity is > 1000 pmoles/min/μg.
- Reconstitution
- Please refer to the printed manual for detailed information.
- Shipping Conditions
- This product is provided as lyophilized powder which is shipped with ice packs.
- Storage Conditions
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
- Calculated Molecular Weight
- 37.1 kDa
- Observed Molecular Weight
- 40 kDa
- Species
- Human