Cathepsin L Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 37.3 kDa and the accession number is A0A024R276.
説明 | Cathepsin L Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 37.3 kDa and the accession number is A0A024R276. |
Species | Human |
Expression Host | HEK293 Cells |
Tag | His |
Accession Number | A0A024R276 |
別名 | MEP, CTSL1, CTSL, cathepsin L, FLJ31037, CATL |
Construction | 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. |
Protein Purity | > 90 % as determined by SDS-PAGE |
分子量 | 37.3 kDa (predicted) |
Endotoxin | < 1.0 EU/μg of the protein as determined by the LAL method. |
Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing 50 mM NaAc, 100 mM NaCl, pH 7.5. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information. |
Stability & Storage |
It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping |
In general, Lyophilized powders are shipping with blue ice. |
Research 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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Cathepsin L Protein, Human, Recombinant (His) MEP CTSL 1 FLJ 31037 CTSL1 CTSL-1 FLJ-31037 CTSL cathepsin L FLJ31037 CATL recombinant recombinant-proteins proteins protein