Adrenomedullin (16-31), human is amino acid residues 16-31 fragment of human adrenomedullin (hADM). Adrenomedullin has appreciable affinity for the CGRP1 receptor. Adrenomedullin (16-31), human possesses pressor activity in the systemic vascular bed of the rat, but not the cat.
CAT No: R1171
CAS No:318480-38-5
Synonyms/Alias:318480-38-5;Adrenomedullin (16-31), human;Adrenomedullin (16-31) (human, pig);DA-70607;FA109167;G12975;H-Cys-Arg-Phe-Gly-Thr-Cys-Thr-Val-Gln-Lys-Leu-Ala-His-Gln-Ile-Tyr-NH2; H-CRFGTCTVQKLAHQIY-NH2;
Adrenomedullin (16-31), human is a synthetic peptide fragment derived from the C-terminal region of the human adrenomedullin protein. Structurally, it represents amino acid residues 16 to 31 of the full-length adrenomedullin sequence, a peptide hormone known for its diverse physiological roles in vascular homeostasis, angiogenesis, and cellular signaling. As a truncated peptide, this fragment retains distinct bioactive properties that make it a valuable research tool for dissecting structure-function relationships within the adrenomedullin family. Its selective sequence composition enables researchers to investigate specific receptor interactions, downstream signaling pathways, and the peptide's influence on biological processes independent of the full-length molecule.
Peptide receptor characterization: Adrenomedullin (16-31), human is widely employed in receptor binding and signaling studies to elucidate the molecular determinants of adrenomedullin receptor activation. By comparing the biological activity of this fragment with that of the full-length peptide, researchers can identify which sequence motifs are essential for high-affinity binding to the calcitonin receptor-like receptor (CRLR) complexed with receptor activity-modifying proteins (RAMPs). Such studies provide critical insights into ligand-receptor specificity, facilitating the design of novel peptide analogs and antagonists for probing adrenomedullin-mediated pathways.
Vascular biology research: The peptide fragment is utilized in experimental models to explore its effects on vascular tone, endothelial cell function, and angiogenic processes. Its ability to modulate vasodilation and vascular permeability, while distinct from the parent peptide, allows for the dissection of domain-specific actions within the adrenomedullin molecule. Researchers leverage these properties to delineate the contribution of different peptide regions to the regulation of blood vessel dynamics, supporting the study of mechanisms underlying vascular homeostasis and remodeling.
Signal transduction studies: Adrenomedullin (16-31), human serves as a molecular probe for investigating intracellular signaling cascades triggered by adrenomedullin receptor engagement. By applying this fragment in cell-based assays, scientists can monitor downstream events such as cyclic AMP production, protein kinase activation, and gene expression changes. These studies help clarify how specific peptide domains influence cellular responses, enabling a more nuanced understanding of adrenomedullin's role in cell signaling networks.
Peptide structure-activity relationship analysis: The defined sequence of adrenomedullin (16-31), human makes it an ideal candidate for structure-activity relationship (SAR) studies. Researchers can systematically modify amino acid residues within this fragment and assess the impact on biological activity, receptor affinity, and stability. Such SAR analyses are instrumental in mapping functional domains, optimizing peptide-based probes, and developing research tools for dissecting complex peptide-receptor interactions.
Peptide synthesis and method development: As a well-characterized fragment, adrenomedullin (16-31), human is frequently utilized as a reference standard or model substrate in peptide synthesis and analytical method validation. Its defined sequence and physicochemical properties support the optimization of solid-phase peptide synthesis protocols, purification strategies, and chromatographic techniques. These applications are particularly valuable for laboratories developing new peptide analogs or establishing robust quality control procedures for research-use peptides.
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