Recombinant Mouse Mast Cell Protease 4 (MCPT4) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03110P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Mast Cell Protease 4 (MCPT4) Protein (His)

Beta LifeScience SKU/CAT #: BLC-03110P
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Product Overview

Description Recombinant Mouse Mast Cell Protease 4 (MCPT4) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P21812
Target Symbol MCPT4
Synonyms Mast cell protease 4; Mcp 4; Mcpt4; MCPT4_MOUSE; MMCP 4; MMCP 4A; MMCP 4B; MMCP-4; MMCP4; MMCP4A; MMCP4B; MSMCP; Myonase; Serosal mast cell protease
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence IIGGVESRPHSRPYMAHLEITTERGFTATCGGFLITRQFVMTAAHCSGREITVTLGAHDVSKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLLCAGVAHGIVSYGRGDAKPPAVFTRISSYVPWINRVIKGE
Expression Range 21-246aa
Protein Length Full Length of Mature Protein
Mol. Weight 29.1kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing.
Protein Families Peptidase S1 family, Granzyme subfamily
Database References

KEGG: mmu:17227

STRING: 10090.ENSMUSP00000038103

UniGene: PMID: 27274047

  • study supports a role for mMCP-4 in the early inflammatory phases of the disease in a mouse model of MS. PMID: 27610007
  • These results suggest that the inhibition of mMCP-4 reduces lesion spreading in the earlier phases of atherosclerosis development and can help stabilise the more advanced plaque PMID: 26976326
  • Results suggest that mouse mast cell proteases 4, 5, and 6 are mediators of the critical role mast cells play in microdeformational wound therapy in the proliferative phase of healing. PMID: 24814421
  • Data indicate that a second-degree burn injury can initiate an immediate novel zonal degranulation of mast cell throughout all skin layers and a disruption of the epidermal tight junctions dependent on the nonredundant presence of mMCP4 and mMCP5. PMID: 24523504
  • these results support the conclusion that mast cells can contribute to the initial lung injury induced by bleomycin through release of the MCPT4 chymase. PMID: 24453258
  • knock-outs demonstrate elevated airway reactivity and eosinophilia, and higher levels of serum immunoglobulin E PMID: 23235745
  • Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation. PMID: 24257755
  • Mast cell released mMCP4 has anti-fibrotic potential in acutely induced obstructive nephropathy. PMID: 23515052
  • Data from Mcp-4 (mast cell protease 4) knockout mice suggest Mcp-4 plays a pivotal role in the dynamic (in vivo and in vitro) conversion of systemic Big-endothelin-1 to endothelin-1 (1-31). PMID: 23596057
  • MCs exert protective functions after trauma, at least in part via mMCP-4, by suppressing exacerbated inflammation via their proteases. PMID: 23193170
  • The effects of interactions between mMCP-4 and TNF in vivo by analyzing the features of a classic model of polymicrobial sepsis, were assessed. PMID: 22901752
  • mMCP-4 plays two different roles in the pathogenesis of experimental BP, by both activating MMP-9 and by cleaving BP180, leading to injury of the hemidesmosomes and extracellular matrix of the basement membrane zone. PMID: 21880713
  • mMCP-4-deficient mice but not to mMCP-5-deficient mice revealing nonredundant actions for these two MC proteases in a model of innate inflammatory injury with remodeling. PMID: 21076070
  • MCP-4 contributes locally to the aggravation of glomerulonephritis by mediating a variety of proinflammatory effects. PMID: 20530261
  • mice deficient in mast cells (Kit(W-sh/W-sh) [Wsh]) or mast cell chymase (Mcpt4(-/-)) have significantly decreased basal small intestinal permeability compared with wild-type (WT) mice PMID: 20018751
  • localization in skeletal muscle myofibrils PMID: 12204111
  • Data describe a mouse strain with a targeted deletion in the gene for mast cell protease 4 (mMCP-4), in terms of tissue localization and functional properties. PMID: 12900518
  • mast cell mMCP-4, -5, and -6 (chymase and tryptase) participate in the acute inflammation and remodeling process of viral myocarditis. PMID: 14578624
  • mast cell chymase and CPA have key roles in both the generation and degradation of Ang II PMID: 15173164
  • key role for mast cell chymase in the regulation of pro-MMP-2 and -9 activities (mast cell chymase AND pro-mmp-2 AND -9) PMID: 15615702
  • Mast cell protease 4 reduces the antibody response and the severity of disease in autoimmune arthritis. PMID: 19010978
  • abdominal aortic aneurysm lesions in Mcpt4(-/-) mice had fewer inflammatory cells and less apoptosis, angiogenesis, and elastin fragmentation than those of WT mice PMID: 19720934
  • chymase (MCP-4) present in the upper airways protects against allergic airway responses, possibly by regulating smooth muscle cells. PMID: 19841188
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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