Mast Cell Protease-1/MCPT-1 Proteins, Antibodies, cDNA Clones Research Reagents

CPT1B (Carnitine Palmitoyltransferase 1B, also known as CPTI; CPT1M; MCPT1; CPT1-M; CPTI-M; M-CPT1; MCCPT1), located on 22q13.33, is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, and frog. The gene produces an 87801 Da protein composed of 772 amino acids. The encoded protein is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. It belongs to the carnitine/choline acetyltransferase family. CPT1B is specific to skeletal muscle, CPT1A is specific to the liver, and CPT1C is specific to the brain.

Mast Cell Protease-1/MCPT-1 Protein (1)

    Mast Cell Protease-1/MCPT-1 Antibody (3)

      Mast Cell Protease-1/MCPT-1 cDNA Clone (13)

      NM_008570.1

      克隆载体 cDNA 产品

      In lentiviral vector

      Mast Cell Protease-1/MCPT-1 qPCR Primer (1)

      Mast Cell Protease-1/MCPT-1 Lysate (1)

        更多受客户欢迎的产品

        Mast Cell Protease-1/MCPT-1 分子背景

        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 the 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 the constitutive release of mMCP-1 by homologs 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 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.

        Mast Cell Protease-1/MCPT-1 参考文献

        • 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.

        Note: Flag® is a registered trademark of Sigma Aldrich Biotechnology LP. It is used here for informational purposes only.