Adrenomedullin (AM) (22-52), human is an adrenomedullin receptor antagonist, and also antagonizes the calcitonin generelated peptide (CGRP) receptor in the hindlimb vascular bed of the cat.
CAT No: R1175
CAS No:159899-65-7
Synonyms/Alias:22-52-Adrenomedullin (human)
Adrenomedullin (AM) (22-52), human is a synthetic peptide fragment derived from the human adrenomedullin protein, corresponding to amino acid residues 22 through 52. As a bioactive segment of the larger adrenomedullin molecule, this peptide retains significant functional motifs associated with receptor binding and signal modulation. Its unique sequence enables selective investigation of adrenomedullin-mediated physiological processes, particularly those related to vascular tone regulation, cellular signaling, and peptide-receptor interactions. Due to these characteristics, the compound has become an important tool in peptide research, enabling detailed analysis of structure-activity relationships and the dissection of receptor subtype specificity within the adrenomedullin system.
Receptor binding studies: The (22-52) fragment of adrenomedullin serves as a valuable ligand for probing the molecular interactions between adrenomedullin and its cognate receptors, such as the calcitonin receptor-like receptor (CRLR) in complex with receptor activity-modifying proteins (RAMPs). By selectively targeting the receptor-binding domain, researchers can employ this peptide to map binding sites, characterize affinity profiles, and elucidate the contributions of specific amino acid residues to receptor engagement. Such studies advance understanding of peptide hormone-receptor dynamics and inform the rational design of analogs with altered pharmacological properties.
Signal transduction research: Utilization of the human AM (22-52) fragment enables precise examination of downstream signaling pathways activated by adrenomedullin receptor engagement. In cellular assays, the peptide can be applied to stimulate or inhibit intracellular cascades, including cyclic AMP production and calcium mobilization, depending on the experimental context. This approach allows researchers to delineate the specific contributions of the central region of adrenomedullin to intracellular events, providing insight into the modulation of vascular smooth muscle cell function, endothelial responses, and related signaling networks.
Vascular biology investigations: Given its well-characterized vasoactive properties, the AM (22-52) peptide is frequently used to study mechanisms of vasodilation, endothelial barrier function, and angiogenesis in vitro and ex vivo. By isolating the effects of the mid-region of adrenomedullin, researchers can distinguish the roles of different peptide domains in mediating endothelial permeability, nitric oxide production, and vascular relaxation. This selective approach facilitates a more nuanced understanding of how adrenomedullin contributes to vascular homeostasis under physiological and pathophysiological conditions.
Peptide structure-activity relationship (SAR) analysis: The human AM (22-52) fragment is instrumental in SAR studies aimed at dissecting the functional domains of adrenomedullin. By comparing the biological activities of truncated peptides, full-length molecules, and site-directed mutants, investigators can identify critical residues responsible for bioactivity, receptor specificity, and stability. Such SAR investigations inform the development of novel peptide analogs with optimized properties for research applications, as well as the design of molecular probes for receptor mapping.
Peptide synthesis and assay development: As a defined peptide fragment, AM (22-52) is frequently employed as a standard or reference compound in the synthesis and analytical validation of adrenomedullin-related peptides. Its use in assay calibration, method development, and quality control ensures reproducibility and accuracy in peptide quantification, receptor screening, and functional testing. The availability of this fragment supports the advancement of peptide-based research tools and enhances the reliability of experimental protocols in both academic and industrial settings.
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