Recombinant Human Cathepsin L2/CTSL2 Protein (His Tag)(Active)
Size: 50μg
Catalogue Number: PKSH031883-50
Citations, Manuals and MSDS Available upon request.
Abbreviation: Cathepsin L2; CTSL2
Target Symptom: Cathepsin L2; Cathepsin U; Cathepsin V; CTSL2; CATL2; CTSU; CTSV
Research Area: Signal Transduction;
Target Species: Human
Expression Host: HEK293 Cells
Application: Enzyme
Fusion Tag: C-His
Accession: NP_001324.2
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.
Activity: 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.
Sequence: Met 1-Val 334
Purity: > 95 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 37.1 kDa
Observed MW: 40 kDa
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Research Use Only