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Recombinant Mouse Cathepsin L/CTSL Protein ( His Tag)

Uniprot : P06797
  • Cat.No.:PKSM040915

  • Expression host: HEK293 Cells

To Purchase PKSM040915

Size:
  • 50µg
Price: $867
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Description

Synonyms Cathepsin L1; Major excreted protein; p39 cysteine proteinase; Ctsl1;1190035F06Rik
Species Mouse
Expression_host HEK293 Cells
Sequence Met 1-Asn 334
Accession P06797
Mol_Mass 37.3 kDa
Tag C-His

Properties

Purity > 90 % as determined by SDS-PAGE
Endotoxin level < 1.0 EU per µg of the protein as determined by the LAL method.
Storage Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile 20mM Tris, 150mM NaCl, pH 7.5
Reconstitution Please refer to the printed manual for detailed information.

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.

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