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. Cathepsin L2 was also expressed by colorectal and breast cancer cell lines as well as by some tumors of diverse origin, including ovarian and renal carcinomas.
Product Name:
Human Cathepsin L2/CTSL2 Recombinant Protein (RPES2203)
Product Code:
RPES2203
Size:
10µg
Species:
Human
Expressed Host:
HEK293 Cells
Synonyms:
Cathepsin L2, Cathepsin U, Cathepsin V, CTSL2, CATL2, CTSU, CTSV
Accession:
NP_001324.2
Sequence:
Met 1-Val 334
Fusion tag:
C-His
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.
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the full length of human cathepsin L2 (NP_001324.2) (Met 1-Val 334) was expressed, with a C-terminal polyhistidine tag.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
37.1 kDa
AP Mol Mass:
40 kDa
Formulation:
Lyophilized from sterile PBS, pH 7.4
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
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.
system_update_altDatasheetHuman Cathepsin L2/CTSL2 Recombinant Protein Cathepsin L2 belongs to the Peptidase C1 family. Cathepsin L2 can be autocatalytically convertedto the mature form as a proe
system_update_altDatasheetHuman Cathepsin A/CTSA Recombinant Protein Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle ma
system_update_altDatasheetHuman Cathepsin Z Recombinant Protein Cathepsin Z (CTSZ); also known as Cathepsin X or CATX; belongs to the C1 family of lysosomal cysteine proteases. Its gene structure
system_update_altDatasheetHuman Cathepsin A/CTSA Recombinant Protein Lysosomal carboxypeptidase, cathepsin A (protective protein, CathA), is a component of the lysosomal multienzyme complex along
system_update_altDatasheetHuman Cathepsin Z Recombinant Protein Cathepsin Z is a lysosomal cysteine proteinase and belongs to the peptidase C1 family. Human Cathepsin Z contains a singnal sequenc
system_update_altDatasheetHuman Cathepsin B/CTSB Recombinant Protein Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes, where it is involved in the turnover o
