|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.
|Mouse MCPT1 ORF mammalian expression plasmid, C-GFPSpark tag||MG50220-ACG|
|Mouse MCPT1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50220-ACR|
|Mouse MCPT1 ORF mammalian expression plasmid, C-Flag tag||MG50220-CF|
|Mouse MCPT1 ORF mammalian expression plasmid, C-His tag||MG50220-CH|
|Mouse MCPT1 ORF mammalian expression plasmid, C-Myc tag||MG50220-CM|
|Mouse MCPT1 ORF mammalian expression plasmid, C-HA tag||MG50220-CY|
|Mouse MCPT1 Gene cDNA clone plasmid||MG50220-M|
|Mouse MCPT1 ORF mammalian expression plasmid, N-Flag tag||MG50220-NF|
|Mouse MCPT1 ORF mammalian expression plasmid, N-His tag||MG50220-NH|
|Mouse MCPT1 ORF mammalian expression plasmid, N-Myc tag||MG50220-NM|
|Mouse MCPT1 ORF mammalian expression plasmid, N-HA tag||MG50220-NY|
|Mouse MCPT1 natural ORF mammalian expression plasmid||MG50220-UT|
|Learn more about expression Vectors|
Mouse Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces constitutive release of mMCP-1 by homologues of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or in systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.