ACTH (1-17), an adrenocorticotropin analogue, is a potent human melanocortin 1 (MC1) receptor agonist with a Ki of 0.21 nM.
CAT No: R1155
CAS No:7266-47-9
Synonyms/Alias:Acth (1-17);alpha1-17-ACTH;7266-47-9;AS-83199;(4S)-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-6-Amino-1-[(2S)-2-[[(2S)-1-[[2-[[(2S)-6-amino-1-[[(2S)-6-amino-1-[[(1S)-4-carbamimidamido-1-carboxybutyl]amino]-1-oxohexan-2-yl]amino]-1-oxohexan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxobutan-2-yl];
ACTH 1-17, also known as Adrenocorticotropic Hormone (1-17), is a synthetic peptide fragment corresponding to the N-terminal 17 amino acids of the full-length ACTH molecule. As a bioactive segment derived from the larger pituitary hormone, it retains significant structural and functional motifs central to ACTH's biological activity, particularly those related to receptor interaction and peptide signaling. Its defined sequence and manageable size make it a valuable tool for dissecting the structure-activity relationships of ACTH and for probing the minimal functional domains necessary for receptor binding and downstream signaling. Because of these properties, ACTH 1-17 is frequently utilized in peptide research, receptor pharmacology, and molecular endocrinology studies.
Peptide-receptor interaction studies: Researchers employ ACTH 1-17 to investigate the specific binding characteristics and activation mechanisms of melanocortin receptors, particularly MC2R, which is the primary receptor for ACTH in adrenal cortical cells. By using this defined fragment, scientists can delineate which portions of the ACTH molecule are essential for receptor recognition and signal transduction. Such studies are fundamental for mapping ligand-receptor interfaces and for understanding the molecular determinants of peptide hormone action.
Structure-activity relationship (SAR) analysis: The defined sequence of ACTH 1-17 serves as a model system for SAR investigations, allowing researchers to systematically modify specific residues or regions within the peptide and assess the resulting impact on biological activity. This approach is critical for identifying key amino acid motifs responsible for receptor activation, peptide stability, and bioactivity. Insights gained from SAR studies with this peptide fragment can inform the rational design of novel analogs or antagonists with tailored properties.
Peptide synthesis and analytical method development: ACTH 1-17 is widely used as a reference standard and test substrate in the optimization of solid-phase peptide synthesis protocols and purification strategies. Its well-characterized sequence and physicochemical properties make it an ideal candidate for validating synthesis efficiency, chromatographic separation methods, and mass spectrometric detection in peptide research laboratories. Such applications are essential for ensuring the reliability and reproducibility of peptide production workflows.
Endocrine signaling pathway research: By utilizing ACTH 1-17 in cellular and biochemical assays, scientists can selectively stimulate or modulate specific signaling cascades downstream of melanocortin receptor activation. This enables targeted exploration of cAMP-mediated pathways, gene expression responses, and secondary messenger systems involved in adrenal physiology and stress response. The use of this peptide fragment allows for controlled studies that minimize confounding effects from other ACTH-derived peptides or full-length hormone.
Immunological assay development: The N-terminal fragment represented by ACTH 1-17 is frequently incorporated into immunoassay platforms for the detection and quantification of ACTH or related peptides in biological samples. Its defined antigenic properties facilitate the generation and validation of antibodies, as well as the calibration of immunoassays designed for research applications. Employing this peptide in assay development supports the advancement of sensitive and specific tools for studying pituitary-adrenal axis regulation and peptide hormone dynamics.
2. TMEM16F and dynamins control expansive plasma membrane reservoirs
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