Overview
- Peptide (C)HSTHPRTDPVGYSRH, corresponding to amino acid residues 201-215 of rat Chemerin receptor 1 (Accession O35786). 2nd extracellular loop.
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- Rat heart and cerebellum (1:200-1:1000).
- Western blot analysis of rat cerebellum lysate (lanes 1 and 3) and rat heart membrane (lanes 2 and 4):1,2. Anti-Rat CMKLR1 (extracellular) antibody (1:200), (ACR-033).
3,4. Anti-Rat CMKLR1 (extracellular) antibody, preincubated with Rat CMKLR1 (extracellular) Blocking Peptide (#BLP-CR033).
Chemerin Receptor 1 belongs to class A G-protein coupled receptors. The receptor is coupled to Gi/o, leading to an increase in intracellular cAMP and Ca2+ following activation by the binding of Chemerin, its endogenous ligand. Like all GPCRs, it has seven transmembrane domains, an extracellular N-terminus and intracellular C-terminal tail1.
Chemerin Receptor 1 has numerous names depending on how the gene encoding the receptor was cloned: Chemokine-like receptor 1, CMKLR1, ChemR23 and others all correspond to the same gene/protein1.
Expression of Chemerin receptor 1 at the mRNA level is largely detected in adipose tissue, and skin dermal layer. At the protein level, CMKLR1 is expressed at the cell surface of dendritic cells, monocytes and macrophages, smooth muscle cells, adipose tissue, lung, lymph nodes and testis1.
A role for the receptor in the inflammatory response has been attributed, however data indicate contradictory roles; proinflammatory and anti-inflammatory functions of the receptor. Expression of Chemerin receptor 1 in adipose tissue clearly establishes its involvement in energy metabolism as an important regulator of adipogenesis1.