|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 is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.
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.
|Mouse CPM ORF mammalian expression plasmid, C-GFPSpark tag||MG50990-ACG|
|Mouse CPM ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50990-ACR|
|Mouse CPM ORF mammalian expression plasmid, C-Flag tag||MG50990-CF|
|Mouse CPM ORF mammalian expression plasmid, C-His tag||MG50990-CH|
|Mouse CPM ORF mammalian expression plasmid, C-Myc tag||MG50990-CM|
|Mouse CPM ORF mammalian expression plasmid, C-HA tag||MG50990-CY|
|Mouse CPM Gene cDNA clone plasmid||MG50990-G|
|Mouse CPM ORF mammalian expression plasmid, N-Flag tag||MG50990-NF|
|Mouse CPM ORF mammalian expression plasmid, N-His tag||MG50990-NH|
|Mouse CPM ORF mammalian expression plasmid, N-Myc tag||MG50990-NM|
|Mouse CPM ORF mammalian expression plasmid, N-HA tag||MG50990-NY|
|Mouse CPM natural ORF mammalian expression plasmid||MG50990-UT|
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Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. CPM in the brain appears to be membrane-bound via a phosphatidylinositol glycan anchor. CPM is widely distributed in a variety of tissues and cells. The amino acid sequence of CPM indicated that the C-terminal hydrophobic region might be a signal for membrane attachment via a glycosylphosphatidylinositol (GPI) anchor. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.