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.
MCP-1/CCL2 Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 15.2 kDa and the accession number is P10148.
MCP-1/CCL2 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 9.79 kDa and the accession number is P61274.
Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa.
Monocyte chemoattractant protein 1 (MCP-1), also called CCL2, is a member of the beta (C-C) subfamily of chemokines that is a chemoattractant for monocytes and basophils but not eosinophils or neutrophils. CCL2 binds the cognate receptor CCR2, and together this signaling pair has been shown to have multiple pro-tumorigenic roles, from mediating tumor growth and angiogenesis to recruiting and usurping host stromal cells to support tumor progression. CCL2 is found in the circulation, where it has been suggested as a diagnostic biomarker of breast cancer and prostate cancer. CCL2 can also induce arachidonic acid release in human monocytes, which has been shown to be involved in adhesion and induction of the chemotactic response, in a pertussis-toxinsensitive manner.
MCP-1/CCL2 Protein, Mouse, Recombinant (His), Biotinylated is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 15.2 kDa and the accession number is P10148.