Galanin (1-16), mouse, porcine, rat (TFA) is an agonist of the hippocampal galanin receptor, with a Kd of 3 nM.
CAT No: R1370
Galanin (1-16), mouse, porcine, rat TFA is a synthetic peptide fragment corresponding to the N-terminal 1-16 amino acids of the galanin neuropeptide sequence, tailored for cross-species research involving murine, porcine, and rat models. As a biologically active peptide, it is structurally derived from native galanin—a neuropeptide widely recognized for its modulatory roles in the central and peripheral nervous systems. The truncated 1-16 fragment retains key residues essential for receptor interaction, making it highly relevant for studies probing the structure-function relationships of galanin and its analogs. Its availability in a trifluoroacetate (TFA) salt form further ensures compatibility with a wide range of biochemical and analytical applications.
Neuropeptide receptor binding studies: Galanin (1-16) serves as a critical tool for characterizing the binding affinities and selectivity profiles of galanin receptors, particularly GALR1 and GALR2 subtypes. By isolating the N-terminal segment, researchers can systematically dissect the minimal structural motifs required for receptor activation or inhibition. This peptide fragment is frequently employed in radioligand binding assays, competitive displacement experiments, and surface plasmon resonance analyses to elucidate the molecular determinants of ligand-receptor interactions within the galaninergic system.
Signal transduction pathway analysis: The use of the 1-16 fragment enables precise investigation of downstream signaling cascades initiated by galanin receptor engagement. Its defined sequence facilitates studies into G-protein coupling, second messenger generation, and phosphorylation events in neuronal and non-neuronal cell models. Researchers leverage this fragment to differentiate the functional consequences of full-length versus truncated galanin peptides, supporting a nuanced understanding of receptor subtype-specific signaling mechanisms.
Peptide structure-activity relationship (SAR) studies: The synthetic galanin (1-16) peptide is instrumental in delineating the structural requirements for biological activity within the galanin family. By comparing the bioactivity of this fragment with longer or modified analogs, scientists can identify critical amino acid residues and conformational features that underlie receptor specificity and efficacy. Such SAR investigations inform rational peptide design for the development of novel ligands, antagonists, or probe molecules targeting galaninergic pathways.
Cross-species comparative neuroscience: The sequence alignment of galanin (1-16) across mouse, porcine, and rat models enables direct comparative studies of neuropeptide function and receptor pharmacology in different mammalian systems. This cross-reactive fragment is particularly valuable in translational research aiming to bridge findings from rodent models to larger mammals, supporting the identification of conserved versus species-specific aspects of galanin-mediated signaling.
Analytical method development: The well-defined sequence and physicochemical properties of galanin (1-16) make it a suitable reference standard for developing and validating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its use as a calibration standard or positive control enhances the accuracy and reproducibility of peptide quantification and detection protocols, supporting rigorous quality assurance in both basic research and biotechnological workflows.
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