C-C motif chemokine 2 (CCL2) is a member of the C-C or β chemokine family. Mouse CCL2 shares 82% amino acid (aa) identity with rat CCL2 over the entire sequence, and 58%, 56%, 55%, 53% and 53% aa identity with human, equine, porcine, bovine and canine CCL2, respectively. Fibroblasts, glioma cells, smooth muscle cells, endothelial cells, lymphocytes and mononuclear phagocytes can produce CCL2 either constitutively or upon mitogenic stimulation, but monocytes and macrophages appear to be the major source. In addition to its chemotactic activity, CCL2 induces enzyme and cytokine release by monocytes, NK cells and lymphocytes, and histamine release by basophils that express its receptor, CCR2. Additionally, it promotes Th2 polarization in CD4+ T cells. CCL2-mediated recruitment of monocytes to sites of inflammation is proposed to play a role in the pathology of atherosclerosis, multiple sclerosis and allergic asthma.

MCP-1/CCL2 Protein, Human, Recombinant (His) is expressed in yeast with His tag. The predicted molecular weight is 10.1 kDa and the accession number is P13500.

The chemokine (C-C motif) receptor 2B (CCR2B) is one of the two isoforms of the receptor for monocyte chemoattractant protein-1 (CCL2), the major chemoattractant for monocytes, involved in an array of chronic inflammatory diseases. The actin-binding protein filamin A (FLNa) as a protein that associates with the carboxyl-terminal tail of CCR2B. FLNa emerges as an important protein for controlling the internalization and spatial localization of the CCR2B receptor in different dynamic membrane structures.

The chemokine (C-C motif) ligand 2 (CCL2), also known as monocyte chemoattractant protein (MCP)-1 and small inducible cytokine A2 (SCYA2)), is a small cytokine that belongs to the CC chemokine family responsible for monocyte attraction. Its cognate receptor, CCR2, play a critical role in regulating nociceptive processes during neuropathic pain. Both CCL2 and CCR2 are implicated in induction of autoimmunity. CCL2 recruits monocytes, memory T cells, and dendritic cells to the sites of inflammation produced by either tissue injury or infection. Recently research also showed that CCL2 might be useful as a biomarker of fibrosis as well as a target for therapeutic intervention.

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.

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, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 11.5 kDa and the accession number is P13500.

MCP-1/CCL2 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 11.5 kDa and the accession number is P13500.

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.

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.

Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. CCL13/MCP-4, is a CC family chemokine that is chemoattractant for eosinophils, basophils, monocytes, macrophages, immature dendritic cells, and T cells, and its capable of inducing crucial immuno-modulatory responses through its effects on epithelial, muscular and endothelial cells. Similar to other CC chemokines, CCL13 binds to several chemokine receptors (CCR1, CCR2 and CCR3), allowing it to elicit different effects on its target cells. A number of studies have shown that CCL13 is involved in many chronic inflammatory diseases, in which it functions as a pivotal molecule involved in the selective recruitment of cell lineages to the inflamed tissues and their subsequent activation. MCP-4/CCL13 is secreted from chondrocytes and activates the proliferation of rheumatoid synovial cells, thereby leading to joint destruction in RA. The interferon-gamma in combination with interleukin-1beta/tumor necrosis factor-alpha activates the production of MCP-4/CCL13 from chondrocytes in RA joints, and that secreted MCP-4/CCL13 enhances fibroblast-like synoviocyte proliferation by activating the extracellular signal-regulated kinase mitogen-activated protein kinase cascade. CCL13 may have some role in the pathogenesis of systemic sclerosis (SSc).

Proto-oncogene tyrosine-protein kinase Yes, also known as Proto-oncogene c-Yes, p61-Yes and YES1, is a cytoplasm protein that belongs to the protein kinase superfamily, Tyr protein kinase family and SRC subfamily. YES1 / c-Yes contains one protein kinase domain, one SH2 domain and one SH3 domain. It is thought that the subcellular distribution of Src-family tyrosine kinases, including c-Yes binding to the cellular membrane, is membranous and/or cytoplasmic. YES1 / c-Yes protein tyrosine kinase is known to be related to malignant transformation. YES1 / c-Yes and c-Src are the two most closely related members of the Src family of nonreceptor tyrosine kinases. Although there is much evidence to support redundancy in signaling between these two kinases. YES1 / c-Yes promotes the formation of the tight junction by phosphorylating occludin, while c-Src signaling downregulates occludin formation in a Raf-1 dependent manner. YES1 / c-Yes has tyrosine kinase activity. It promotes infectivity of Neisseria gonorrhoeae in epithelial cells by phosphorylating MCP / CD46.

Pre-B cell colony enhancing factor (PBEF) was originally identified as a cytokine that potentiated the clonal expansion and differentiation of pre-B cells, but it is also acknowledged to be the ubiquitous intracellular enzyme nicotinamide phosphoribosyltranferase (NAMPT) and the adipokine “visfatin”. PBEF is constitutively expressed in the fetal membranes where its greatest expression is in the amnion. It has intracellular and extracellular forms. Most of the intracellular functions of PBEF are due to its role as a Nampt which can induce angiogenesis through upregulation of VEGF and VEGFR and secretion of MCP-1. Extracellular PBEF has been shown to increase inflammatory cytokines, such as TNF-α, IL-1β, IL-16, and TGF-β1. PBEF also increases the production of IL-6, TNF-α, and IL-1β in CD14+ monocyctes, macrophages, and dendritic cells, enhances the effectiveness of T cells.

CD46, also known as Membrane Cofactor Protein (MCP), is a complement regulatory protein. CD46 is a type 1 membrane protein that plays an important inhibitory role in the complement system. CD46 is expressed in white blood cells, platelets, epithelial cells, and fibroblasts. Human CD46 shares 5% amino acid sequence identity with mouse and rat CD46. The importance of CD46 to complement regulation is underscored by the observation that genetic loss of CD46 leads to development of atypical hemolytic-uremic syndrome (aHUS), a disease characterized by uncontrolled complement activation. CD46 is implicated in the development and/or progression of selected cancer types.

MCP-2 Protein, Human, Recombinant (SUMO) is expressed in E. coli expression system with SUMO tag. The predicted molecular weight is 21.7 kDa and the accession number is P80075-1.

Ccl12 prevented initiation of the reparative response by prolonging inflammation and inhibiting fibroblast conversion to myofibroblasts, resulting in diminished scar formation. Macrophage secretion of Ccl12 directly impaired fibronectin and collagen deposition and indirectly stimulated collagen degradation through upregulation of matrix metalloproteinase-2. In post-MI patients, circulating LPS levels strongly associated with the Ccl12 homologue monocyte chemotactic protein 1 (MCP-1). Both MCP-1 and MCP-5 are HIF-1 target genes and that HIF-1alpha is involved in transcriptional induction of these two chemokines in astrocytes by hypoxia.