Anti-CCR2/CD192 Polyclonal Antibody

The C-C motif chemokine receptor-2 (CCR2) is a G protein-coupled receptor (GPCR), made up of a carboxy-terminus, extracellular amino terminus, and a hydrophobic transmembrane domain consisting of 7 amino acid segments that mediates agonist-dependent calcium mobilization and inhibition of adenylyl cyclase. CCR2 is expressed on monocytes, immature dendritic cells, and T-cell subpopulations, and mediates their migration towards endogenous CCL2. CCR2 is necessary for macrophage-dependent inflammatory responses and the development of atherosclerosis. In mice, CCR2 deficiency reduced macrophage content, increased adiponectin expression, ameliorated hepatic steatosis, and improved systemic glucose homeostasis and insulin sensitivity. Resistance to HIV-1 infection or delayed progression to AIDS may be linked to CCR2 polymorphisms. Furthermore, CCR2 mRNA was highly expressed in prostate cancer (PCa) metastatic tissues compared with benign prostate tissues according to real-time RT-PCR3, suggesting that CCR2 may contribute to PCa development. Protein function: Key functional receptor for CCL2 but can also bind CCL7, and CCL12 (PubMed:23408426, PubMed:38157855, PubMed:8048929, PubMed:8146186). Also transduces signaling mediated by CCL13 (PubMed:38157855). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (PubMed:38157855). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (PubMed:23938203). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation. Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression, signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R. Plays an important role in mediating peripheral nerve injury-induced neuropathic pain. Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B. Mediates the recruitment of macrophages and monocytes to the injury site following brain injury. [The UniProt Consortium]