|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Human CTSL1 ORF mammalian expression plasmid, C-GFPSpark tag||HG10486-ACG|
|Human CTSL1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10486-ACR|
|Human CTSL1 ORF mammalian expression plasmid, C-Flag tag||HG10486-CF|
|Human CTSL1 ORF mammalian expression plasmid, C-His tag||HG10486-CH|
|Human CTSL1 ORF mammalian expression plasmid, C-Myc tag||HG10486-CM|
|Human CTSL1 ORF mammalian expression plasmid, C-HA tag||HG10486-CY|
|Human CTSL1 Gene cDNA clone plasmid||HG10486-M|
|Human CTSL1 ORF mammalian expression plasmid, N-Flag tag||HG10486-NF|
|Human CTSL1 ORF mammalian expression plasmid, N-His tag||HG10486-NH|
|Human CTSL1 ORF mammalian expression plasmid, N-Myc tag||HG10486-NM|
|Human CTSL1 ORF mammalian expression plasmid, N-HA tag||HG10486-NY|
|Human CTSL1 natural ORF mammalian expression plasmid||HG10486-UT|
|Learn more about expression Vectors|
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.