Cathepsin L Protein (His tag)

Produktnummer ABIN7194682

Dieses Recombinant Cathepsin L-Protein wird in HEK-293 Cells exprimiert.

Kurzübersicht für Cathepsin L Protein (His tag) (ABIN7194682)

Target: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Protein-Typ: Recombinant

Biologische Aktivität: Active

Spezies: Human

Quelle: HEK-293 Cells

Reinheit: > 90 % as determined by reducing SDS-PAGE.

Produktdetails

Aufreinigungstag / Konjugat: Dieses Cathepsin L Protein ist gelabelt mit His tag.

Verwendungszweck: Recombinant Human Cathepsin L/CTSL Protein (His Tag)(Active)

Sequenz: Met 1-Val 333

Produktmerkmale: A DNA sequence encoding the pro form of human Cathepsin-L1 (NP_001903.1) (Met 1-Val 333) was expressed, fused with a polyhistidine tag at the C-terminus.

Endotoxin-Niveau: < 1.0 EU per μg as determined by the LAL method.

Biological Activity Comment: Measured by its binding ability in a functional ELISA. Immobilized human CD74 at 5 μg/ml (100 μl/well) can bind biotinylated human CTSL1 with a linear range of 3.2-400 ng/ml.

Anwendungsinformationen

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Lyophilized

Rekonstitution: Please refer to the printed manual for detailed information.

Buffer: Lyophilized from sterile 50 mM NaAc, 0.1M NaCl, pH 5.0

Lagerung: 4 °C,-20 °C,-80 °C

Informationen zur Lagerung: Generally, 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°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Antigendetails

Target: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Andere Bezeichnung: Cathepsin L/CTSL

Hintergrund:

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.

Synonym: Cathepsin L1, Major Excreted Protein, MEP, CTSL1, CTSL

Molekulargewicht: 37.3 kDa

NCBI Accession: NP_001903

Pathways: Activation of Innate immune Response, Toll-Like Receptors Cascades