|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|Rat CTSL1 ORF mammalian expression plasmid, C-GFPSpark tag||RG80646-ACG|
|Rat CTSL1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||RG80646-ACR|
|Rat CTSL1 ORF mammalian expression plasmid, C-Flag tag||RG80646-CF|
|Rat CTSL1 ORF mammalian expression plasmid, C-His tag||RG80646-CH|
|Rat CTSL1 ORF mammalian expression plasmid, C-Myc tag||RG80646-CM|
|Rat CTSL1 ORF mammalian expression plasmid, C-HA tag||RG80646-CY|
|Rat CTSL1 ORF mammalian expression plasmid, N-Flag tag||RG80646-NF|
|Rat CTSL1 ORF mammalian expression plasmid, N-His tag||RG80646-NH|
|Rat CTSL1 ORF mammalian expression plasmid, N-Myc tag||RG80646-NM|
|Rat CTSL1 ORF mammalian expression plasmid, N-HA tag||RG80646-NY|
|Rat CTSL1 Gene cDNA clone plasmid||RG80646-U|
|Rat CTSL1 natural ORF mammalian expression plasmid||RG80646-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.