Relaxin Family Related Drug Discovery Products
Creative Biolabs has the assays you can rely on for high throughput screening, lead optimization, characterizing and discovering targets, and uncovering the complexity of disease pathways. We can offer membrane protein in vitro assay kits that save valuable laboratory time and is ideal for high throughput screening.
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
One of the earliest peptide hormones to be identified was relaxin. In fact, relaxin is produced as a pre-prohormone that has a signal sequence and a B-C-A domain arrangement, just like insulin. The mature protein is created by removing the C chain and three disulfide bonds forming between six highly conserved cysteine residues on the A and B chains. The conserved residues are mostly restricted to the cysteine residues that form an intra-chain disulfide bond within the A chain and connect the A and B domains by two inter-chain disulfide bonds, as well as the nearby glycine residues, in all species. All relaxin peptides share a conserved amino acid pattern in the B-chain that is essential for their interaction with the relaxin receptor.
Creative Biolabs is proud to offer our clients a series of relaxin family related tools with the best quality and most competitive price:
Overview of Relaxin Family
- RXFP1 and RXFP2
Similar to the rhodopsin receptor, RXFP1 and RXFP2 are family A GPCRs that specifically belong to the leucine-rich repeat-containing GPCR (LGR) subfamily. The RXFP1 and RXFP2 genes are enormous. RXFP1 and RXFP2 have 29 known splice variants, which can produce a variety of different protein products, including fragments that only have the transmembrane or extracellular region of the protein. The majority of the transmembrane-containing variants expressed at the cell surface are not ligand-binding. However, an RXFP2 variant that is only missing the exon that encodes the LDLa module can bind ligand but does not cause the production of cAMP, indicating that this variant may be a native binding protein that could modify the action of INSL3 in vivo. Therefore, by binding to and preventing relaxin from activating RXFP1, these variants might function as functional RXFP1 antagonists.
- RXFP3 and RXFP4
Small peptide receptors, which share a relatively short NH2-terminal domain with family A GPCRs, are most closely related to RXFP3 and RXFP4. RXFP3 and RXFP4 are much smaller than RXFP1 and RXFP2 as a result of this short NH2-terminal domain. The genes do not have any splice variants since they lack introns, unlike RXFP1 and RXFP2. RXFP3 and RXFP4 share a close relationship with the chemokine receptor CCR1, the angiotensin II type 1 receptor (AGTR1), the apelin receptor (APLNR), and a second subgroup of neuropeptide receptors that includes members of the somatostatin and opioid receptor families as well as the neuropeptide B/W receptor (NPBWR1). The cognate ligands for these receptors are very similar to one another, although the RXFP1/RXFP2 and RXFP3/RXFP4 receptor subgroups are not very linked to one another.
Relaxin Family Drug Discovery
Understanding how the ligands bind to and activate the receptors has advanced quickly since the discovery of the relaxin family peptide receptors. Understanding the intricate activation processes of RXFP1 and RXFP2 is essential for developing drugs that target these receptors. While relaxin is currently undergoing Phase III trials for the treatment of acute heart failure, all of the peptides exhibit excellent therapeutic potential. Since these peptides cannot be taken orally and are unlikely to cross the blood brain barrier even when administered intravenously, small molecule mimics of these peptides are crucial for further clinical development. Therefore, more research on the interactions between ligands and receptors is necessary for structure-based drug design.
