Overview
- Peptide (C)RKTVLSKAIEKIK, corresponding to amino acid residues 336-348 of rat prostanoid EP4 receptor (Accession P43114). Intracellular, C-terminus.
- Rat brain membranes, mouse lung lysate, human THP-1 monocytic leukemia, and human Jurkat T-cell leukemia cell lysates (1:200-1:2000).
- Western blot analysis of rat brain membranes (lanes 1 and 3) and mouse lung lysate (lanes 2 and 4):1,2. Anti-Prostaglandin E Receptor EP4 (PTGER4) Antibody (#APR-066), (1:200).
3,4. Anti-Prostaglandin E Receptor EP4 (PTGER4) Antibody, preincubated with Prostaglandin E Receptor EP4/PTGER4 Blocking Peptide (#BLP-PR066). - Western blot analysis of human THP-1 monocytic leukemia cell line lysate (lanes 1 and 3) and human Jurkat T-cell leukemia cell line lysate (lanes 2 and 4):1,2. Anti-Prostaglandin E Receptor EP4 (PTGER4) Antibody (#APR-066), (1:400).
3,4. Anti-Prostaglandin E Receptor EP4 (PTGER4) Antibody, preincubated with Prostaglandin E Receptor EP4/PTGER4 Blocking Peptide (#BLP-PR066).
- Human blood eosinophils (Durchschein, F. et al. (2019) Dig. Dis. Sci. 64, 2806.).
E-type prostanoid receptor 4 (EP4) is responsible for mediating the effects of prostaglandin E2 (PGE2), an endogenous molecule involved in several biological processes such as pain, fever, regulation of vascular tone, renal function, mucosal integrity, inflammation, angiogenesis and tumor growth. In turn, EP4 receptor is involved in anti-inflammatory, anti-thrombotic, vasoprotective effects, adverse tumor-promoting and pro-angiogenic roles1,2.
EP4 mRNA expression is detected in the gastrointestinal tract, uterus, hematopoietic tissues and skin. High expression is also found in most immune cell types. The EP receptors activate various signaling pathways. EP4 is a Gs coupled receptor, which activates adenylate cyclase and activates intracellular cyclic adenylyl monophosphate (cAMP) production1,2.
The EP receptors contain an aspartate in the second transmembrane domain, which is involved in receptor-ligand interaction and conserved cysteine residues in the second and third extracellular domains, which form a disulfide bonds critical for stabilizing the receptor and for ligand binding3.