Abcam, ab58991, Anti-Cathepsin L/MEP antibody

Size: 200µL
Rabbit Polyclonal CPL1 antibody. Suitable for WB and reacts with Caenorhabditis elegans samples. Cited in 37 publications.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Caenorhabditis elegans,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Specificity:Reacts specifically with Cathepsin L/MEP protease 36 kDa wild type protein of C.elegans

Properties and Storage Information:
Form-Liquid, Purity-Whole antiserum, Storage buffer-Constituents: Whole serum, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

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.