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Mouse MCPT1 Protein (His Tag)

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Mouse MCPT1 Protein Product Information
Synonym:Mcpt1, AV080368, Mcp-1
Protein Construction:A DNA sequence encoding the mouse MCPT1 (NP_032596.1) (Met 1-Lys 246) was expressed with a polyhistidine tag at the C-terminus.
Expressed Host:Human Cells
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Mouse MCPT1 Protein QC Testing
Purity:> 97 % as determined by SDS-PAGE
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Glu 19
Molecule Mass:The secreted recombinant mouse MCPT1 consists of 239 amino acids and has a predicted molecular mass of 26.8 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm MCPT1 is approximately 32-34 kDa due to glycosylation.
Formulation:Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Mouse MCPT1 Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Mouse MCPT1 Protein SDS-PAGE
Mouse MCPT1 Protein (His Tag) SDS-PAGE
Other MCPT1 Recombinant Protein Products
MCPT1 Background

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.

Mouse MCPT1 References
  • Pemberton AD, et al. (2003) Purification and characterization of mouse mast cell proteinase-2 and the differential expression and release of mouse mast cell proteinase-1 and -2 in vivo. Clin Exp Allergy. 33(7): 1005-12.
  • Brown JK, et al. (2003) Constitutive secretion of the granule chymase mouse mast cell protease-1 and the chemokine, CCL2, by mucosal mast cell homologues. Clin Exp Allergy. 33(1): 132-46.
  • Lawrence CE, et al. (2004) Mouse mast cell protease-1 is required for the enteropathy induced by gastrointestinal helminth infection in the mouse. Gastroenterology. 127(1): 155-65.
  • Pemberton AD, et al. (2006) Anaphylactic release of mucosal mast cell granule proteases: role of serpins in the differential clearance of mouse mast cell proteases-1 and -2. J Immunol. 176(2): 899-904.
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    Catalog: 50220-M08H-10
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    All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.