Cathepsin L [60616-82-2]
16-12-030112
Protein IDP07711
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameCathepsin L [60616-82-2]
- Delivery Days Customer9
- Applications SupplierCancer, SARS-CoV-2, Emphysema, Atherosclerosis, In Vitro Diagnostic
- CertificationResearch Use Only
- Estimated Purity≥ 95% by SDS-PAGE
- Protein IDP07711
- Protein NameProcathepsin L
- Scientific DescriptionCathepsin L (CTSL) is one of the most potent lysosomal cysteine endopeptidases, demonstrating significantly higher specific activity than cathepsins B and H in degrading physiological protein substrates. As a member of the papain-like protease family, CTSL plays crucial roles in protein catabolism, antigen processing, bone resorption, and ovulation. CTSL is widely expressed in eukaryotic cells, functioning primarily within lysosomes but also secreted extracellularly. It efficiently degrades various substrates including extracellular matrix proteins (laminins, fibronectin, collagens), cytoplasmic, and nuclear proteins. CTSL exhibits specificity for aromatic residues in the P2 position with limited prime-site selectivity4. CTSL is significantly upregulated in multiple cancer types, particularly breast cancer, where it serves as a powerful predictor of relapse and survival following treatment. Its ability to degrade extracellular matrix facilitates tumor invasion and metastasis. CTSL plays key roles in, coronary heart disease progression SARS-CoV-2 infection, and pulmonary emphysema development. CTSL represents a promising therapeutic target, with inhibitors showing potential in preventing cancer metastasis, treating COVID-19 by blocking viral entry mechanisms, and managing atherosclerosis progression
- Shelf life instructionmore then 1 year
- SourcePrepared from liver shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
- Storage Instruction≤ -80° C
- UNSPSC41116100
References
- Lambeth, T. R., et al., (2021), 'Proteolysis of Amyloid bèta by Lysosomal Enzymes as a Function of Fibril Morphology', ACS Omega, 6: pp 31520−31527.Read this paper
- Sanman, L. E., et al., (2016), 'Bifunctional Probes of Cathepsin Protease Activity and pH Reveal Alterations in Endolysosomal pH during Bacterial Infection', Cell Chemical Biology, 23(7): pp 793 - 804.Read this paper
- Mellott, D. M., et al., (2021), 'A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV‑2 Infection of Human and Monkey Cells', ACS Chem. Biol., 16: pp 642−650.Read this paper