Endothelin-1 is a 21 amino acid polypeptide with effective vasoconstriction. Activates phospholipase C in fibroblasts expressing ETA receptors. Endothelin-1 autocrine and paracrine signal transduction regulates cell proliferation, apoptosis, migration, and epithelial to mesenchymal transition, suggesting its role in cancer.
CAT No: R1818
CAS No:117399-94-7
Synonyms/Alias:Endothelin 1;117399-94-7;ENDOTHELIN 1 HUMAN, PORCINE;C109H159N25O32S5;CSCSSLMDKECVYFCHLDIIW;Endothelin-1 (human, porcine);Endothelin-1 (human, bovine, dog, mouse, porcine, rat) acetate salt;H-Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-Glu-Cys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-Ile-Trp-OH; H-CSCSSLMDKECVYFCHLDIIW-OH;HB3442;AKOS024456425;DA-52897;FE110251;G12353;(Disulfide bridge between 1 - 15, 3 - 11);Endothelin 1, Human and Porcine - CAS 117399-94-7;Endothelin-1 (human, bovine, dog, mouse, porcine, rat) trifluoroacetate salt;
Endothelin 1, human, porcine, is a potent vasoconstrictive peptide belonging to the endothelin family, characterized by its 21-amino acid sequence and distinctive disulfide-bonded structure. Synthesized in vascular endothelial cells, this peptide plays a central role in modulating vascular tone, cellular proliferation, and various signaling pathways across mammalian systems. The human and porcine forms of Endothelin 1 exhibit high sequence homology, making the compound particularly valuable for comparative studies in cardiovascular physiology and translational research. Its ability to bind and activate endothelin receptors (ETA and ETB) underpins a wide array of experimental applications in vascular biology, smooth muscle research, and cell signaling investigations.
Vascular physiology research: As a reference peptide for studying vasoconstriction, Endothelin 1 is extensively utilized in in vitro and ex vivo models to elucidate mechanisms of blood vessel contraction and regulation. Researchers employ it to induce controlled vasoconstrictive responses in isolated artery rings or perfused organ systems, enabling detailed analysis of endothelial function, receptor pharmacology, and the effects of candidate vasoactive compounds. Its robust and reproducible action on smooth muscle cells provides a reliable tool for dissecting the molecular underpinnings of vascular tone regulation.
Receptor pharmacology: The peptide serves as a critical ligand in studies of endothelin receptor signaling, enabling precise characterization of ETA and ETB receptor subtype selectivity, affinity, and downstream signaling cascades. By applying Endothelin 1 to cultured cells or tissue preparations, investigators can probe receptor-mediated calcium mobilization, second messenger activation, and cross-talk with other G protein-coupled receptor pathways. Such research is instrumental in identifying novel antagonists, agonists, or modulators targeting the endothelin system, with implications for understanding cardiovascular and renal pathophysiology.
Cell proliferation and remodeling: Endothelin 1 is frequently employed to investigate its mitogenic effects on vascular smooth muscle cells, fibroblasts, and cardiac myocytes. Its capacity to stimulate cellular proliferation, migration, and extracellular matrix synthesis makes it a valuable tool for modeling vascular remodeling, fibrosis, and tissue repair processes in vitro. Researchers use it to delineate the signaling pathways—such as MAPK, PI3K/Akt, and Rho kinase—that govern cell growth and structural adaptation in response to peptide stimulation.
Signal transduction studies: The peptide is widely adopted for dissecting intracellular signaling mechanisms triggered by endothelin receptor activation. Experimental protocols often include its application to assess phosphorylation events, transcription factor activation, and gene expression changes in various cell types. These studies contribute to a deeper understanding of how endothelin signaling integrates with other cellular networks, influences oxidative stress responses, and modulates inflammatory mediators in cardiovascular and non-cardiovascular tissues.
Comparative and translational research: The high degree of conservation between human and porcine Endothelin 1 sequences facilitates cross-species investigations, particularly in preclinical models. Researchers utilize the peptide to bridge findings from animal studies to human systems, enhancing the translational relevance of vascular, renal, and pulmonary research. Its utility extends to comparative pharmacology, where it serves as a benchmark for evaluating the efficacy and specificity of new endothelin-targeting compounds across different mammalian models, thus informing drug discovery and mechanistic studies in the field of endothelial biology.
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