Anti-Cathepsin L/CTSL1 antibody

Cat.#: 102452

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Product Information

  • Product Name
    Anti-Cathepsin L/CTSL1 antibody
  • Documents
  • Description
    Rabbit polyclonal to Cathepsin L/CTSL1
  • Tested applications
    ELISA, WB
  • Species reactivity
    Human Cathepsin-L1 / CTSL1
  • Alternative names
    1190035F06Rik antibody; Cathepsin L antibody; Cathepsin L antibody; Cathepsin L1 antibody; Cathepsin L1 antibody; CATL antibody; Ctsl antibody; CTSL antibody; Ctsl1 antibody; CTSL1 antibody; FLJ31037 antibody; fs antibody; MEP antibody; nkt antibody; Mep antibody; MEP antibody; CATL antibody; CTSL1 antibody; fs antibody; MEP antibody; nkt antibody; Ctsl1 antibody; 1190035F06Rik antibody
  • Immunogen
  • Isotype
    Rabbit IgG
  • Preparation
    Produced in rabbits immunized with purified, recombinant Human Cathepsin-L1 / CTSL1 (rh CTSL1; NP_001903.1; Met 1-Val 333). CTSL1 specific IgG was purified by human CTSL1 affinity chromatography.
  • Clonality
    Polyclonal
  • Formulation
    0.2 μm filtered solution in PBS with 5% trehalose
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    WB: 10-20 μg/mL

    ELISA: 0.5-1 μg/mL

    This antibody can be used at 0.5-1 μg/mL with the appropriate secondary reagents to detect Human CTSL. The detection limit for Human CTSL is approximately 0.0049 ng/well.

  • Validations

  • 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 diagnostic 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.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"