Overview
- Peptide CFPLHYDQAEDFGSR, corresponding to amino acid residues 556-570 of mouse RXFP2 (Accession Q91ZZ5). 2nd extracellular loop.
- Rat testis, rat brain, mouse testis and mouse brain membranes (1:400-1:2000).
Western blot analysis of rat brain (lanes 1 and 5), rat testis (lanes 2 and 6), mouse brain (lanes 3 and 7) and mouse testis (lanes 4 and 8):1-4. Anti-RXFP2 (extracellular) Antibody (#ARR-012), (1:400).
5-8. Anti-RXFP2 (extracellular) Antibody, preincubated with RXFP2 (extracellular) Blocking Peptide (#BLP-RR012).
Relaxin (RXFP) peptides are members of a family of peptide hormones, structurally related to insulin, which act on a group of four G-protein-coupled receptors known as Relaxin family peptide receptors (RXFPs): RXFP1–4.
The RXFP2 (also called LGR8) structure contains 7-transmemebrane spanning domains, at least two binding sites: a long extracellular sequence with a high affinity site containing 10 leucine-rich repeat region and a lower-affinity site in an extracellular loop of a transmembrane region. In addition, the receptor contains an N-terminal ectodomain that acts as a site of primary ligand binding1,2. RXFP2 is also the native receptor for insulin-like peptide 3 (INSL3)1,2. Activation of the receptor leads to increased levels of cAMP.
In human, RXFP2 can be detected in the uterus, testis, kidney, brain, thyroid, muscle, peripheral blood cells and bone marrow. Additional expression in rat and mouse was detected in the ovary and gubernaculums.
Studies show that activators of RXFP2 may play an important role in the treatment of cryptorchidism and infertility and RXFP2 inhibitors could be used as a means of contraception1. RXFP2 also was found to cause the failure of gubernacular development during embryogenesis in human and mouse3.
