Adrenomedullin (1-50), rat is a 50 amino acid peptide, which induces a selective arterial vasodilation via activation of CGRP1 receptor.
CAT No: R1170
Adrenomedullin (1-50), rat is a synthetic peptide corresponding to the full-length sequence of rat adrenomedullin, a multifunctional regulatory peptide originally identified in the adrenal medulla. As a member of the calcitonin gene-related peptide (CGRP) family, it is characterized by a 52-amino acid structure in most mammals, with this product comprising the first 50 residues. Adrenomedullin exhibits a broad spectrum of biological activities, including vasorelaxation, angiogenesis, and modulation of cellular proliferation. Its significance extends to diverse physiological systems, making it a valuable tool for elucidating peptide-mediated signaling pathways, vascular homeostasis, and receptor pharmacology in experimental settings.
Peptide signaling research: As a potent endogenous vasodilatory peptide, adrenomedullin is widely employed in studies investigating G protein-coupled receptor (GPCR) signaling, particularly focusing on the calcitonin receptor-like receptor (CRLR) and its receptor activity-modifying proteins (RAMPs). Researchers utilize this peptide to dissect downstream signaling cascades, such as cyclic AMP (cAMP) production and nitric oxide synthesis, providing insights into the molecular mechanisms underlying vascular tone regulation and tissue perfusion. Its use facilitates the characterization of ligand-receptor specificity and the identification of novel modulators of peptide hormone activity.
Vascular biology investigations: The functional properties of adrenomedullin make it a critical reagent in experimental models of vascular physiology and pathology. It is frequently applied in assays assessing endothelial cell function, angiogenic responses, and vascular permeability. By modulating key processes such as endothelial proliferation, migration, and barrier integrity, the peptide enables researchers to explore the molecular underpinnings of vascular development, remodeling, and responses to injury or hypoxia. These studies contribute to a deeper understanding of peptide-driven vascular adaptations and their implications in health and disease.
Peptide structure-activity relationship (SAR) studies: The defined sequence of adrenomedullin (1-50), rat provides an essential standard for SAR analyses aimed at mapping functional domains within the peptide. By serving as a reference or comparator in assays with truncated, mutated, or modified analogs, it allows for the systematic evaluation of residue-specific contributions to receptor binding, bioactivity, and stability. Such investigations inform the rational design of peptide mimetics, antagonists, or agonists with tailored pharmacological profiles, advancing both basic and applied peptide science.
Receptor pharmacology and antagonist screening: The peptide is instrumental in in vitro and ex vivo assays designed to probe the pharmacological properties of adrenomedullin receptors. By acting as a selective agonist, it enables the quantification of receptor activation, desensitization, and internalization dynamics. Furthermore, it serves as a benchmark for screening small molecules, antibodies, or peptide-based antagonists that modulate adrenomedullin signaling, supporting drug discovery efforts targeting peptide hormone pathways.
Peptide synthesis and analytical validation: As a well-characterized bioactive peptide, adrenomedullin (1-50), rat is routinely utilized as a reference standard in peptide synthesis and analytical method development. Its defined sequence and established activity profile make it suitable for calibrating chromatographic, mass spectrometric, and immunochemical assays. This application ensures the accuracy and reproducibility of quantitative measurements in peptide research, quality control, and process optimization workflows.
4. Emu oil in combination with other active ingredients for treating skin imperfections
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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