Cathepsin V Active Protein | CTSV active protein

Cathepsin V Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8119993

• Gene Names: CTSV; CTSU; CATL2; CTSL2
• Purity: >95% as determined by SDS-PAGE
• Synonyms: Cathepsin V; Cathepsin V Protein; Human; Recombinant (His Tag); Human Cathepsin V/Cathepsin L2/Preproprotein Protein (His Tag); CATL2 Protein; CTSL2 Protein; CTSU Protein; CTSV Protein; MGC125957 Protein; cathepsin V; CTSV active protein

• Host: HEK293 Cells
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Val334

• Species: Human
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Val 18
• Tag: C-His
• 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.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Activity: Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC. The specific activity is >1000pmoles/min/ug.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for CTSV active protein

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. 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.

References

Itoh R, et al. (1999) Genomic organization and chromosomal localization of the human cathepsin L2 gene. DNA Res. 6(2): 137-40.Tolosa E, et al. (2003) Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis. J Clin Invest. 112(4): 517-26.Yasuda Y, et al. (2004) Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J Biol Chem. 279(35): 36761-70.Puzer L, et al. (2008) Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen. Biol Chem. 389(2): 195-200.

NCBI and Uniprot Product Information

• NCBI GI #: 23110960
• NCBI GeneID: 1515
• NCBI Accession #: NP_001324.2
• NCBI GenBank Nucleotide #: NM_001333.3
• UniProt Accession #: O60911; O60233; Q2TB86; Q5T1U0
• Molecular Weight: 37,329 Da
• NCBI Official Full Name: cathepsin L2 preproprotein
• NCBI Official Synonym Full Names: cathepsin V
• NCBI Official Symbol: CTSV
• NCBI Official Synonym Symbols: CTSU; CATL2; CTSL2
• NCBI Protein Information: cathepsin L2; cathepsin U; cathepsin L2, preproprotein
• UniProt Protein Name: Cathepsin L2
• UniProt Gene Name: CTSL2
• UniProt Synonym Gene Names: CATL2; CTSU; CTSV
• UniProt Entry Name: CATL2_HUMAN

NCBI Description

The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may play an important role in corneal physiology. This gene is expressed in colorectal and breast carcinomas but not in normal colon, mammary gland, or peritumoral tissues, suggesting a possible role for this gene in tumor processes. Alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jan 2011]

Uniprot Description

CTSL2: Cysteine protease. May have an important role in corneal physiology. Belongs to the peptidase C1 family.

Protein type: Protease; Secreted; Secreted, signal peptide; EC 3.4.22.15

Chromosomal Location of Human Ortholog: 9q22.2

Cellular Component: extracellular space; lysosomal lumen; neuron projection; microvillus; apical part of cell; extracellular region; nucleolus; perikaryon; secretory granule; external side of plasma membrane

Molecular Function: protein binding; histone binding; cysteine-type endopeptidase activity; protein complex binding; aminopeptidase activity; kininogen binding; cysteine-type carboxypeptidase activity; peptide binding; cysteine-type peptidase activity

Biological Process: extracellular matrix organization and biogenesis; hair follicle morphogenesis; response to glucocorticoid stimulus; Sertoli cell differentiation; multicellular organismal aging; antigen processing and presentation of exogenous peptide antigen via MHC class II; decidualization; proteolysis; cellular response to starvation; extracellular matrix disassembly; protein autoprocessing; response to glucose stimulus; autophagic cell death; nerve development; spermatogenesis