Cathepsin L Recombinant Protein | CTSL recombinant protein

Cathepsin L Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120310

• Gene Names: CTSL1; MEP; CATL; CTSL; FLJ31037; CTSL1
• Purity: >90% as determined by SDS-PAGE
• Synonyms: Cathepsin L; Cathepsin L Protein; Human; Recombinant (His Tag); Human Cathepsin L1/CTSL1 Protein (His Tag); CATL Protein; CTSL Protein; CTSL1 Protein; FLJ31037 Protein; MEP Protein; cathepsin L; CTSL recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >90% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 50mM NaAc, 100mM NaCl, pH7.5. 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-Val333

• Species: Human
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Thr 18
• Tag: C-His
• Protein Construction: A DNA sequence encoding the pro form of human Cathepsin-L1 (NP_001903.1)(Met 1-Val 333) was expressed, fused with a polyhistidine tag at the C-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• 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 CTSL recombinant protein

Background: Cathepsin L is a lysosomal cysteine protease that plays a major role in intracellular protein catabolism, and is potent in degrading collagen, laminin, elastin, as well as alpha-1 protease inhibitor and other structural proteins of basement membranes. It is secreted by liver flukes at all stages of their development in the mammalian host, are believed to play important roles in facilitating parasite migration (tissue degradation), feeding and immuno-evasion. Like many proteases, Cathepsin L is synthesized as an inactive preproenzyme, and cleavage of the 96-residue proregion is necessary to generate the fully active 221-residue mature enzyme. Studies have demonstrated that cleavage of the proregion occur autocatalytically under acidic conditions. The enzyme takes part in nutrient acquisition by catabolizing host proteins to absorbable peptides, facilitates the migration of the parasite through the host intestine and liver by cleaving interstitial matrix proteins such as fibronectin, laminin and native collagen and is implicated in the inactivation of host immune defenses by cleaving immunoglobulins. Recently, Cathepsin L has been shown to suppress Th1 immune response in infected laboratory animals making them susceptible to concurrent bacterial infections. Cathepsin L is synthesized in large amounts and secreted by many malignantly transformed cells, and induced by growth factors and tumor promoters. In addition to its role in protein degradation, evidence has accumulated for the participation of Cathepsin L in various physiological and pathological processes, such as tumor invasion and metastasis, bone resorption, spermatogenesis, and arthritis. Accordingly, Cathepsin L may prove useful as a test or prognostic marker of human tumor malignancy.

References

Mulcahy G, et al. (2001) Cathepsin L proteinases as vaccines against infection with Fasciola hepatica (liver fluke) in ruminants. Res Vet Sci. 70(1): 83-6.Dixit AK, et al. (2008) Immunodiagnostic/protective role of cathepsin L cysteine proteinases secreted by Fasciola species. Vet Parasitol. 154(3-4): 177-84.Leto G, et al. (2010) Cathepsin L in metastatic bone disease: therapeutic implications. Biol Chem. 391(6): 655-64.

NCBI and Uniprot Product Information

• NCBI GI #: 4503155
• NCBI GeneID: 1514
• UniProt Accession #: P07711; Q6IAV1; Q96QJ0
• NCBI Official Full Name: cathepsin L1 preproprotein [Homo sapiens]
• NCBI Official Synonym Full Names: cathepsin L1
• NCBI Official Symbol: CTSL1
• NCBI Official Synonym Symbols: MEP; CATL; CTSL; FLJ31037; CTSL1
• UniProt Protein Name: Cathepsin L1
• Protein Family: Cathepsin
• UniProt Gene Name: CTSL1
• UniProt Synonym Gene Names: CTSL; MEP
• UniProt Entry Name: CATL1_HUMAN

Uniprot Description

CTSL1: Important for the overall degradation of proteins in lysosomes. Belongs to the peptidase C1 family.

Protein type: Motility/polarity/chemotaxis; EC 3.4.22.15; Protease

Chromosomal Location of Human Ortholog: 9q21.33

Cellular Component: extracellular space; lysosomal lumen; lysosome; extracellular region; nucleus

Molecular Function: collagen binding; protein binding; proteoglycan binding; histone binding; fibronectin binding; cysteine-type endopeptidase activity; cysteine-type peptidase activity

Biological Process: antigen processing and presentation; extracellular matrix disassembly; collagen catabolic process; extracellular matrix organization and biogenesis; adaptive immune response; proteolysis involved in cellular protein catabolic process; toll-like receptor signaling pathway; innate immune response; antigen processing and presentation of exogenous peptide antigen via MHC class II; proteolysis