|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 CTRL ORF mammalian expression plasmid, C-GFPSpark tag||HG13748-ACG|
|Human CTRL ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG13748-ACR|
|Human CTRL ORF mammalian expression plasmid, C-Flag tag||HG13748-CF|
|Human CTRL ORF mammalian expression plasmid, C-His tag||HG13748-CH|
|Human CTRL ORF mammalian expression plasmid, C-Myc tag||HG13748-CM|
|Human CTRL ORF mammalian expression plasmid, C-HA tag||HG13748-CY|
|Human CTRL Gene cDNA clone plasmid||HG13748-G|
|Human CTRL ORF mammalian expression plasmid, N-Flag tag||HG13748-NF|
|Human CTRL ORF mammalian expression plasmid, N-His tag||HG13748-NH|
|Human CTRL ORF mammalian expression plasmid, N-Myc tag||HG13748-NM|
|Human CTRL ORF mammalian expression plasmid, N-HA tag||HG13748-NY|
|Human CTRL natural ORF mammalian expression plasmid||HG13748-UT|
|Learn more about expression Vectors|
CTRL-1, also known as chymotrypsin-like protease, belongs to the peptidase S1 family. CTRL-1 contains 1 peptidase S1 domain. Its expression is increased in preeclampsia (PE). Placental-derived chymotrypsin-like protease is responsible for inducing endothelial inflammatory phenotypic changes possibly by upregulation of cell adhesion molecule expressions, activation of cellular protease, and induction of extracellular regulated kinase phosphorylation. Activated microglia have been observed in various neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and multiple sclerosis. Five structurally distinct inhibitors that are known to inhibit chymotrypsin-like proteases were partially protective. They might represent a novel class of drugs with benefit in diseases where overactivity of microglia contributes to the pathogenesis.