Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 2 bp deletion in exon 2
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-CTSL, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Cathepsin L also known as CTSL is a protease enzyme that has a mass of approximately 29-30 kDa. It originates from the peptidase C1 family and undergoes activation in acidic environments. This protein carries out proteolytic processes by breaking down proteins through cleaving peptide bonds. Cathepsin L has various forms including MEP (a common alternate name) and MEP L and it expresses itself in organs such as the liver kidney and spleen as well as in tumors and immune cells. It has a significant functional role in lysosomes where it degrades proteins.
Biological function summary
Cathepsin L links to cellular homeostasis and extracellular matrix remodeling. It often acts in protein turnover and antigen processing within endolysosomal compartments making it essential for major histocompatibility complex class II presentation. Cathepsin L forms complexes in certain conditions playing roles in interacting and modifying other proteins. It controls processes essential for cell survival differentiation and apoptosis.
Pathways
Cathepsin L plays significant roles in pathways like apoptosis and autophagy. It coordinates with other proteases and proteins such as cathepsin B and cathepsin S to regulate cell death and survival. In apoptosis cathepsin L mediates the breakdown of cellular components working alongside caspases. Its interaction with autophagy involves degradation of long-lived proteins highlighting its role in recycling amino acids during stress conditions.
Cathepsin L connects strongly to cancer and fibrotic diseases. It contributes to tumor progression and metastasis due to its ability to degrade the extracellular matrix and enable cancer cell invasion. In fibrosis cathepsin L modulates the turnover of fibrous tissue linking to the development of lung fibrotic diseases. Proteins like collagenases work in concert with cathepsin L during these pathological processes to remodel tissues underlining its implication in disease states.
