Calcitonin Gene Related Peptide (CGRP) (83-119), rat (TFA) is a 37 amino acid calcitonin family of neuropeptide, acts through calcitonin receptor-like receptor (CRLR).
CAT No: R1262
Calcitonin Gene Related Peptide (CGRP) (83-119), rat TFA is a synthetic peptide fragment corresponding to residues 83-119 of the rat calcitonin gene-related peptide sequence, provided as a trifluoroacetate salt. As a neuropeptide of significant interest in neurobiology and vascular physiology, CGRP plays a crucial role in modulating vasodilation, neurotransmission, and pain signaling. Its highly conserved structure and functional activity in rodents make it an essential tool for dissecting the molecular mechanisms underlying migraine, nociception, and cardiovascular regulation. Researchers utilize this peptide fragment to model native CGRP activity in vitro and in vivo, facilitating the study of receptor interactions, signal transduction pathways, and the physiological consequences of peptide-receptor engagement.
Neuroscience research: The peptide serves as a model agonist in studies of sensory neuron function and neuropeptide signaling. By applying CGRP (83-119) to cultured dorsal root ganglion neurons or central nervous system preparations, investigators can probe the molecular pathways involved in neurogenic inflammation, synaptic plasticity, and pain processing. Its use enables detailed analysis of CGRP receptor activation, downstream cAMP-mediated effects, and the modulation of ion channel activity, supporting the elucidation of pain transmission mechanisms relevant to migraine and neuropathic pain models.
Vascular biology studies: CGRP is a well-established vasodilator, and the rat-derived peptide fragment is widely used to investigate the regulation of vascular tone and endothelial function. Application of this peptide to isolated artery or vein preparations allows for the assessment of endothelium-dependent and -independent relaxation responses, helping to clarify the roles of G protein-coupled receptors and secondary messengers in vascular smooth muscle cells. Such studies provide valuable insights into the mechanisms of blood flow regulation and the pathophysiology of hypertension and other cardiovascular disorders.
Receptor pharmacology: The peptide fragment is instrumental in characterizing the pharmacological properties of CGRP receptors, including binding affinity, selectivity, and signal transduction profiles. Through radioligand binding assays, competition studies, and functional bioassays, researchers can evaluate the impact of novel antagonists, receptor mutants, or signaling modulators. These investigations are critical for advancing understanding of receptor-ligand interactions and for the development of new molecular probes or tool compounds targeting the CGRP pathway.
Peptide structure-function analysis: As a defined fragment of the full-length neuropeptide, CGRP (83-119) enables systematic studies of structure-activity relationships. By comparing the biological activities of this sequence with those of truncated or modified analogs, scientists can identify key residues responsible for receptor binding, activation, and signal specificity. Such structure-function analyses inform rational design of peptide mimetics and contribute to the broader understanding of neuropeptide-receptor interactions.
Peptide synthesis and assay development: The availability of this synthetic rat peptide fragment supports the development and validation of bioanalytical assays, such as ELISA or mass spectrometry-based quantitation of CGRP in biological samples. It acts as a standard or positive control for assay calibration, ensuring reproducibility and accuracy in quantifying endogenous peptide levels. This application is particularly important in preclinical research settings, where precise measurement of neuropeptide concentrations is required to correlate physiological responses with molecular signaling events.
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