|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Mouse CTSL was immunoprecipitated using:
Lane A:0.5 mg A549 Whole Cell Lysate2 µL anti-Mouse CTSL rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-Mouse CTSL rabbit polyclonal antibody,at 1:100 dilutionSecondary antibody:
Dylight 800-labeled antibody to rabbit IgG (H+L), at 1:5000 dilutionDeveloped using the odssey technique.
Performed under reducing conditions.Predicted band size: 38 kDa
Observed band size: 38 kDa
Anti-CTSL rabbit polyclonal antibody at 1:500 dilution
Lane A: U87MG Whole Cell Lysate
Lane B: NIH3T3 Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:38 kDa
Observed band size:38 kDa
(We are unsure as to the identity of these extra bands.)
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 diagnostic or prognostic marker of human tumor malignancy.
|Product Description||Host||Clonality||Application||Catalog# (PDF)|
|Anti-Cathepsin L Antibody||Rabbit||Polyclonal||ELISA||50015-RP01|
|Anti-Cathepsin L Antibody||Rabbit||Monoclonal||WB||10486-R221|
|Anti-Cathepsin L Antibody||Rabbit||Monoclonal||ELISA||10486-R002|
|Anti-Cathepsin L Antibody||Rabbit||Polyclonal||ELISA||10486-RP01|
|Anti-Cathepsin L Antibody||Rabbit||Polyclonal||WB,ELISA||10486-RP02|
|Anti-Cathepsin L Antibody||Mouse||Monoclonal||ELISA||10486-MM07|