Adrenocorticotropic Hormone (ACTH) (1-10), human, an adrenocorticotropin hormone fragment, possesses a weak α-melanocyte stimulating hormone (α-MSH) potency only at high doses (100 and 1000 nM).
CAT No: R1162
CAS No:2791-05-1
Synonyms/Alias:Acth (1-10);2791-05-1;Acth(1-10);EX-A7457;HY-P1518;MS-32100;PD099876;Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly;CS-0044637;
Adrenocorticotropic Hormone (ACTH) (1-10), human is a synthetic peptide fragment corresponding to the amino-terminal sequence of the full-length human ACTH protein. As a decapeptide, it represents the first ten amino acids of ACTH, a key polypeptide hormone involved in the regulation of the adrenal cortex and the hypothalamic-pituitary-adrenal (HPA) axis. This fragment retains partial biological activity and is widely studied for its structure-function relationships, receptor interactions, and signaling mechanisms. Its defined sequence and biochemical properties make it a valuable research tool in peptide science, endocrinology, and neurobiology.
Peptide structure-activity relationship studies: The ACTH (1-10) fragment is frequently utilized to dissect the minimal structural requirements for receptor binding and biological activity of ACTH-derived peptides. By comparing the effects of this decapeptide with longer or full-length ACTH analogs, researchers can map critical residues necessary for melanocortin receptor activation and downstream signaling. Such investigations contribute to a deeper understanding of peptide-receptor interactions and inform the rational design of selective agonists or antagonists.
Receptor binding assays: In molecular pharmacology and biochemistry, ACTH (1-10) serves as a reference ligand for characterizing binding affinities and selectivity profiles of melanocortin receptors, especially MC2R and related subtypes. Its defined sequence allows for precise quantification of receptor-ligand interactions in radioligand binding studies, fluorescence polarization, or surface plasmon resonance assays. These applications are essential for elucidating receptor pharmacodynamics and for screening novel modulators of the melanocortin system.
Peptide synthesis and analytical method development: The decapeptide is a standard substrate in the development and validation of solid-phase peptide synthesis protocols. Its sequence complexity and physicochemical properties make it suitable for optimizing coupling strategies, purification methods, and analytical techniques such as high-performance liquid chromatography (HPLC) or mass spectrometry. As a model peptide, it supports quality control and method benchmarking in peptide manufacturing and analytical laboratories.
Neuroendocrine signaling research: ACTH (1-10) is employed in experimental models to study neuropeptide signaling within the central nervous system and peripheral tissues. Its application enables the investigation of peptide-mediated modulation of neuronal activity, synaptic plasticity, and neuroendocrine feedback mechanisms. By isolating the effects of specific ACTH fragments, researchers can delineate distinct physiological roles and signaling pathways associated with the HPA axis and related neuropeptide systems.
Immunological and bioassay development: The human ACTH (1-10) fragment is also employed in the development of immunoassays and bioanalytical platforms for peptide quantification. Its defined epitope structure facilitates the generation of specific antibodies and calibration standards, supporting the accurate detection and measurement of ACTH-related peptides in research samples. These applications underpin studies in endocrinology, stress physiology, and biomarker discovery, offering reliable tools for peptide quantification and functional analysis.
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