Adrenomedullin(1-52) is a 52-amino acid peptide with multi-functions. It was originally isolated from pheochromocytoma and adrenal medulla but is widely distributed throughout the body including lung and kidney tissues. Besides controlling fluid-electrolyte homeostasis, adrenomedullin is a potent vasodilator and can inhibit pituitary ACTH secretion.
CAT No: R1864
CAS No:148498-78-6
Synonyms/Alias:Human adrenomedullin;Adrenomedullin (human);148498-78-6;Adrenomedullin;Human adrenomedullin(1-52);Human adrenomedullin-(1-52)-NH2;DA-70610;FA108807;Adrenomedullin (human) trifluoroacetate salt;
Adrenomedullin (1-52), human is a biologically active peptide that serves as the full-length, mature form of adrenomedullin found in human tissues. As a member of the calcitonin gene-related peptide (CGRP) superfamily, it is characterized by a unique ring structure and C-terminal amidation, conferring stability and distinct receptor interactions. This peptide is widely recognized for its multifaceted regulatory functions in vascular biology, cellular signaling, and homeostatic processes. Its ability to interact with specific G protein-coupled receptors and modulate intracellular pathways makes it a valuable tool in advanced biochemical and physiological research.
Vascular biology research: Adrenomedullin (1-52) is frequently employed in studies investigating the mechanisms of vasodilation, endothelial function, and vascular tone regulation. Researchers use this peptide to elucidate the molecular basis of blood vessel relaxation, permeability, and angiogenesis, taking advantage of its potent activity on vascular smooth muscle cells and endothelial cells. Its application facilitates the exploration of nitric oxide-dependent and cAMP-mediated signaling cascades, which are crucial for understanding cardiovascular homeostasis and the pathogenesis of vascular disorders.
Receptor pharmacology: The full-length peptide is an essential reagent for characterizing the pharmacological properties of adrenomedullin receptors, particularly the calcitonin receptor-like receptor (CLR) in complex with receptor activity-modifying proteins (RAMPs). By enabling ligand-binding assays, signal transduction studies, and receptor activation profiling, it allows for precise dissection of receptor subtype specificity and downstream effectors. This contributes to a deeper understanding of GPCR family signaling and aids in the identification of novel modulators or antagonists targeting these pathways.
Cellular signaling pathway analysis: In cellular and molecular biology, adrenomedullin peptides are used to probe intracellular signaling networks, including cAMP-PKA, MAPK, and PI3K-Akt pathways. Application of the human peptide in in vitro systems supports the mapping of downstream phosphorylation events, gene expression changes, and cross-talk with other hormonal or stress-response networks. Such studies are instrumental in uncovering the peptide's pleiotropic effects on cell growth, migration, and survival, particularly in endothelial and smooth muscle cell models.
Inflammation and immune modulation studies: The peptide's regulatory influence on immune cells and inflammatory mediators has prompted its use in research focused on innate and adaptive immune responses. Investigators utilize the compound to assess its impact on cytokine production, leukocyte migration, and barrier function within tissue models. These applications are particularly relevant for exploring the molecular mechanisms underlying inflammatory diseases, tissue injury, and immune cell trafficking.
Peptide structure-function analysis: As a well-characterized endogenous peptide, adrenomedullin (1-52), human is often used as a reference standard in structure-activity relationship (SAR) studies. Researchers synthesize analogs or truncated versions of the molecule to delineate the contributions of specific amino acid residues and structural motifs to receptor binding, bioactivity, and metabolic stability. These structure-function investigations provide critical insights for peptide engineering, receptor mapping, and the rational design of novel bioactive compounds with improved selectivity or stability profiles.
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