PEN (rat) is a neuropeptide fragment characterized by a mixture of hydrophobic, aromatic, and basic side chains that support receptor association. The sequence adopts flexible conformations that can stabilize helical or extended states depending on environment. Researchers study its role in neuroendocrine signaling models and receptor-binding assays. Applications include peptide-hormone motif analysis, structure-function research, and analog design.
CAT No: R2607
CAS No:569364-13-2
Synonyms/Alias:PEN (rat);569364-13-2;L-Valine,L-alanyl-L-valyl-L-a-aspartyl-L-glutaminyl-L-a-aspartyl-L-leucylglycyl-L-prolyl-L-a-glutamyl-L-valyl-L-prolyl-L-prolyl-L-a-glutamyl-L-asparaginyl-L-valyl-L-leucylglycyl-L-alanyl-L-leucyl-L-leucyl-L-arginyl-;AKOS032962866;DA-66557;PD080178;
PEN (rat), also known as rat proenkephalin-derived peptide, is a synthetic peptide corresponding to a sequence found in the rat proenkephalin precursor protein. As a member of the opioid peptide family, PEN is of significant interest in neurobiology and peptide research due to its involvement in modulating neurotransmission, pain perception, and various neuroendocrine processes. Its defined amino acid sequence and origin from endogenous opioid pathways make it a valuable tool for dissecting the molecular mechanisms of peptide signaling in rodent models. The biochemical properties of PEN enable researchers to explore receptor interactions, signaling cascades, and the physiological roles of enkephalin-derived peptides in the central nervous system.
Neuropharmacology research: PEN (rat) is widely used in neuropharmacological studies to investigate the function of opioid peptides in the central nervous system. By applying this peptide to in vitro or ex vivo models, researchers can characterize its effects on opioid receptor subtypes, elucidate downstream signaling pathways, and assess its influence on synaptic transmission. These studies contribute to a deeper understanding of how endogenous opioid peptides regulate neuronal excitability, pain modulation, and behavioral responses in rodent systems.
Receptor binding assays: In receptor pharmacology, the peptide serves as a reference ligand for binding assays targeting delta and mu opioid receptors. Its defined sequence allows for precise quantification of binding affinity and receptor selectivity, facilitating the screening and characterization of novel opioid ligands or antagonists. By employing PEN in competitive binding experiments, scientists can map receptor-ligand interactions and advance the development of pharmacological tools for opioid research.
Peptide structure-function analysis: The use of PEN (rat) in structure-function studies enables detailed examination of the molecular determinants underlying opioid peptide activity. Through site-directed mutagenesis, analog synthesis, or biophysical characterization, researchers can probe the relationship between sequence motifs, receptor recognition, and biological function. Insights gained from these studies inform the rational design of peptide analogs with tailored pharmacological profiles for research applications.
Neuropeptide signaling investigations: The peptide is instrumental in dissecting the roles of proenkephalin-derived fragments in neuropeptide signaling networks. By applying it to neuronal cultures or tissue preparations, investigators can monitor downstream signaling events such as second messenger activation, ion channel modulation, or gene expression changes. These experiments help clarify the contribution of specific peptide fragments to the broader landscape of neuropeptide-mediated communication in the brain and peripheral tissues.
Peptide standard for analytical methods: In analytical biochemistry, PEN (rat) is utilized as a standard or reference compound for the development and validation of peptide quantification methods. Its defined composition and stability make it suitable for calibrating mass spectrometry, HPLC, or immunoassay platforms aimed at detecting endogenous or synthetic opioid peptides in biological samples. The use of this peptide as a calibrant enhances the accuracy and reproducibility of quantitative analyses in peptide research and neurochemical profiling.
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