Motilin (26-47), human, porcine is an endogenous motilin receptor ligand with Ki and EC50 of 2.3 nM and 0.3 nM in a Chinese hamster ovary cell line.
CAT No: R1516
CAS No:52906-92-0
Synonyms/Alias:52906-92-0;Motilin (26-47), human, porcine;MOTILIN;CHEMBL411576;PML-4147-V;BDBM50143037;DA-55645;
Motilin (26-47), human, porcine is a synthetic peptide fragment derived from the C-terminal region of motilin, a gastrointestinal peptide hormone. Comprising amino acids 26 through 47 of the native motilin sequence, this fragment is highly conserved between human and porcine species, making it a valuable tool for comparative and cross-species studies. The peptide plays a significant role in gastrointestinal motility regulation and is of particular interest in research focused on gut peptide signaling, receptor-ligand interactions, and peptide structure-activity relationships. Its well-characterized sequence and functional relevance have established it as a key reagent in studies aiming to elucidate the physiological and molecular mechanisms underlying gastrointestinal peptide function.
Peptide receptor binding studies: Researchers frequently utilize the Motilin (26-47) fragment to investigate the binding specificity and affinity of motilin receptors, particularly the G protein-coupled motilin receptor (MLNR). By employing this peptide in ligand-receptor interaction assays, scientists can dissect the minimal active region required for receptor activation, map critical binding domains, and evaluate species-specific receptor pharmacology. Such studies are essential for advancing the understanding of gut hormone signaling pathways and for informing the rational design of receptor agonists or antagonists.
Structure-activity relationship (SAR) analysis: The truncated C-terminal fragment serves as a model system for exploring the structural determinants of motilin's biological activity. Through comparative assays involving full-length and partial peptides, researchers can identify the essential amino acid residues and secondary structural motifs that govern receptor activation and downstream signaling. These SAR investigations provide valuable insights into the molecular basis of peptide hormone function and support the development of novel peptide analogs with tailored bioactivity profiles.
Peptide synthesis and method development: Motilin (26-47), human, porcine is frequently employed as a reference standard or model substrate in peptide synthesis laboratories. Its defined sequence and moderate length make it suitable for optimizing solid-phase peptide synthesis protocols, evaluating coupling efficiencies, and benchmarking purification strategies. The peptide's use in method development helps ensure reproducibility and quality control in the production of research-grade peptides for diverse applications.
Comparative species studies: The high degree of sequence conservation between human and porcine motilin (26-47) fragments enables their use in comparative physiology and evolutionary biology research. By analyzing the functional responses of the peptide across different mammalian systems, investigators can assess interspecies similarities and differences in motilin signaling, contributing to a deeper understanding of gastrointestinal regulatory mechanisms and evolutionary adaptation of peptide hormones.
Analytical assay calibration: Laboratories also employ this motilin fragment as a calibration standard in analytical platforms such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized physicochemical properties facilitate the validation of peptide detection, quantification, and purity assessment methods. Reliable assay calibration using this peptide supports accurate measurement of motilin and related peptides in complex biological samples, enhancing the rigor and reproducibility of peptide quantification studies.
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