Prolactin Releasing Peptide (12-31), human is a fragment of the prolactin releasing peptide (PrRP). Prolactin Releasing Peptide (1-31), human is a high affinity GPR10 ligand that cause the release of the prolactin.
CAT No: R1633
CAS No:235433-36-0
Synonyms/Alias:235433-36-0;Prolactin-Releasing Peptide (12-31) (human);L-Phenylalaninamide, L-threonyl-L-prolyl-L-alpha-aspartyl-L-isoleucyl-L-asparaginyl-L-prolyl-L-alanyl-L-tryptophyl-L-tyrosyl-L-alanyl-L-seryl-L-arginylglycyl-L-isoleucyl-L-arginyl-L-prolyl-L-valylglycyl-L-arginyl-;CHEMBL5082678;215510-22-8;MFCD02094631;BDBM50583783;NCGC00167183-01;DA-77086;FP109256;FP109260;G13102;H-Ser-Arg-Thr-His-Arg-His-Ser-Met-Glu-Ile-Arg-Thr-Pro-Asp-Ile-Asn-Pro-Ala-Trp-Tyr-Ala-Ser -Arg-Gly-Ile-Arg-Pro-Val-Gly-Arg-Phe-NH2; H-SRTHRHSMEIRTPDINPAWYASRGIRPVGRF-NH2;H-Thr-Pro-Asp-Ile-Asn-Pro-Ala-Trp-Tyr-Ala-Ser-Arg-Gly-Ile-Arg-Pro-Val-Gly-Arg-Phe-NH2; H-TPDINPAWYASRGIRPVGRF-NH2;
Prolactin Releasing Peptide (12-31), human, is a synthetic peptide fragment corresponding to amino acids 12 through 31 of the human prolactin-releasing peptide (PrRP) sequence. As a bioactive segment derived from the endogenous neuropeptide PrRP, it is recognized for its role in modulating neuroendocrine functions, particularly those related to prolactin secretion. The peptide's specific sequence enables selective interaction with PrRP receptors, making it a valuable molecular tool for dissecting receptor-mediated signaling pathways. Its relevance extends to studies of hypothalamic regulation, neuropeptide receptor pharmacology, and the broader field of peptide hormone research, where precise fragments are required to probe structure-activity relationships and functional mechanisms.
Neuroendocrine signaling research: Prolactin Releasing Peptide (12-31), human, is widely utilized in studies exploring the mechanisms of neuroendocrine signaling within the hypothalamus and pituitary axis. Researchers employ this fragment to investigate how specific regions of the PrRP molecule contribute to prolactin release and regulation. By applying the peptide to cultured pituitary cells or hypothalamic explants, scientists can assess its capacity to induce or modulate prolactin secretion, thereby delineating the role of distinct peptide domains in neurohormonal control.
Receptor pharmacology and binding studies: The peptide serves as a critical tool for mapping the interaction between PrRP and its cognate G protein-coupled receptors (notably GPR10). By using this defined fragment in receptor binding assays, researchers can determine the minimal structural requirements for high-affinity receptor activation or antagonism. These studies support the development of receptor subtype-selective ligands and facilitate detailed characterization of ligand-receptor specificity, which is essential for advancing the understanding of neuropeptide receptor pharmacology.
Structure-activity relationship (SAR) analysis: Prolactin Releasing Peptide (12-31), human, is instrumental in SAR investigations aimed at identifying the functional residues and motifs responsible for biological activity. Through systematic substitution, truncation, or modification of this peptide segment, scientists can evaluate how alterations affect receptor binding and downstream signaling. Such SAR studies are foundational for the rational design of novel peptide analogs with optimized activity profiles for research applications.
Peptide synthesis and analytical method development: The defined sequence of this peptide fragment makes it an important reference standard and substrate in peptide synthesis protocols. It is frequently used to validate synthetic strategies, optimize purification processes, and calibrate analytical instrumentation such as HPLC and mass spectrometry. The availability of a well-characterized peptide standard supports quality assurance in peptide production and analytical method development within research laboratories.
Functional assays in neurobiology: In experimental neurobiology, Prolactin Releasing Peptide (12-31), human, is applied in functional assays to elucidate the physiological and behavioral outcomes of PrRP signaling. Researchers utilize the peptide to probe its effects on neuronal activity, neurotransmitter release, and neuroendocrine feedback mechanisms in both in vitro and ex vivo systems. These functional studies contribute to a deeper understanding of how PrRP fragments influence central nervous system processes, providing insight into the broader roles of neuropeptides in brain function and behavior.
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