|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 F11 / FXI ORF mammalian expression plasmid, C-GFPSpark tag||HG10302-ACG|
|Human F11 / FXI ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10302-ACR|
|Human F11 / FXI ORF mammalian expression plasmid, C-Flag tag||HG10302-CF|
|Human F11 / FXI ORF mammalian expression plasmid, C-His tag||HG10302-CH|
|Human F11 / FXI ORF mammalian expression plasmid, C-Myc tag||HG10302-CM|
|Human F11 / FXI ORF mammalian expression plasmid, C-HA tag||HG10302-CY|
|Human F11 / FXI Gene cDNA clone plasmid||HG10302-M|
|Human F11 / FXI ORF mammalian expression plasmid, N-Flag tag||HG10302-NF|
|Human F11 / FXI ORF mammalian expression plasmid, N-His tag||HG10302-NH|
|Human F11 / FXI ORF mammalian expression plasmid, N-Myc tag||HG10302-NM|
|Human F11 / FXI ORF mammalian expression plasmid, N-HA tag||HG10302-NY|
|Human F11 / FXI natural ORF mammalian expression plasmid||HG10302-UT|
|Learn more about expression Vectors|
Factor XI (plasma thromboplastin antecedent) is a plasma glycoprotein, and a zymogen acting as a serine protease which participates in blood coagulation as a catalyst in the conversion of factor IX to factor IXa in the presence of calcium ions. It is an unusual dimeric protease, with structural features that distinguish it from vitamin K-dependent coagulation proteases. The factor XI is synthesized in the liver as a single polypeptide chain with a molecular weight estimated between 125 ~160 kDa and then is processed into a disulfide-bond linked homodimer. FXI is a homodimer, with each subunit containing four apple domains and a protease domain. The apple domains form a disk structure with binding sites for platelets, high molecular weight kininogen, and the substrate factor IX (FIX). FXI is converted to the active protease FXIa by cleavage of the Arg369-Ile370 bond on each subunit. After the activation reaction, Factor XIa is composed of two heavy and two light chains held together by three disulfide bonds. The heavy chains are derived from the amino termini of the zymogen and responsible for the binding of factor XI to high molecular weight kininogen and for the activation of factor IX, while the light chain contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases. FXI deficiency is a disorder characterized by a mild or no bleeding tendency. Severe FXI deficiency is an injury-related bleeding disorder common in Ashkenazi Jews and rare worldwide.