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Recombinant Human Cathepsin L2/CTSL2 Protein (His Tag)(Active)– MSE Supplies LLC

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Recombinant Human Cathepsin L2/CTSL2 Protein (His Tag)(Active)

SKU: PKSH031883-50

  • $ 78095



Recombinant Human Cathepsin L2/CTSL2 Protein (His Tag)(Active)

 

SKU # PKSH031883
Expression Host HEK293 Cells

 

 

Description

Synonyms CATL2, CTSL2, CTSU, CTSV, Cathepsin L2, Cathepsin U, Cathepsin V
Species Human
Expression Host HEK293 Cells
Sequence Met 1-Val 334
Accession NP_001324.2
Calculated Molecular Weight 37.1 kDa
Observed Molecular Weight 40 kDa
Tag C-His
Bio-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.
  

 

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
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.
Formulation Lyophilized from sterile PBS, pH 7.4
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 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.



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.