Adrenocorticotropic Hormone (ACTH) (18-39), human is a corticotropinlike intermediate lobe peptide, which is produced in the melanotrophs of the intermediate lobe of the pituitary.
CAT No: R1166
CAS No:53917-42-3
Synonyms/Alias:CLILP;CLIP;53917-42-3;Acth(18-39);Acthalpha(18-39), serine(31)-;31-Ser-acthalpha(18-39);Corticotropin-like intermediate lobe peptide;Corticotropin-like intermediate lobe peptide (human);Acthalpha(18-39), ser(31)-;CLIP (ACTH 18-39);Corticotropin Like Intermediate Lobe Peptide;
Adrenocorticotropic Hormone (ACTH) (18-39), human, is a synthetic peptide fragment derived from the C-terminal region of the full-length human ACTH polypeptide. This segment comprises amino acids 18 through 39 and is distinct from the biologically active N-terminal region responsible for stimulating adrenal steroidogenesis. As a truncated peptide, ACTH (18-39) lacks intrinsic corticotropic activity but retains structural features relevant to peptide mapping, receptor binding studies, and the investigation of pro-opiomelanocortin (POMC) processing. Its unique sequence and lack of direct hormonal activity make it valuable for dissecting the roles of ACTH domains in biochemical and physiological contexts.
Peptide mapping and structural studies: The ACTH (18-39) fragment is frequently employed in peptide mapping protocols to elucidate the structural properties and conformational dynamics of the POMC-derived peptides. By isolating and characterizing this specific region, researchers can investigate the post-translational modifications, folding patterns, and sequence-specific interactions that contribute to the overall function of ACTH and its related peptides. Such studies enable a deeper understanding of peptide structure-activity relationships and facilitate the development of analytical methods for peptide identification and quantification.
Receptor binding assays: Although the 18-39 fragment does not activate the melanocortin 2 receptor (MC2R) responsible for adrenal steroidogenesis, it serves as a critical control or competitor in receptor binding assays. Utilizing this peptide allows for the differentiation between specific and nonspecific binding events, helping to clarify the binding affinities and selectivity profiles of full-length ACTH and related analogs. This approach supports the characterization of receptor-ligand interactions and advances the pharmacological understanding of the melanocortin receptor family.
Immunoassay development: The ACTH (18-39) peptide is utilized in the development and validation of immunoassays designed to detect and quantify ACTH or its fragments in biological samples. Its defined sequence and lack of hormonal activity make it an ideal standard or negative control for assay specificity testing, antibody cross-reactivity assessment, and calibration purposes. Employing this fragment enhances assay accuracy and reliability in both research and diagnostic workflows focused on POMC-derived peptides.
Peptide synthesis and analytical method validation: As a well-characterized synthetic peptide, ACTH (18-39) is instrumental in validating peptide synthesis protocols and optimizing purification processes. It serves as a model substrate for evaluating chromatographic techniques, mass spectrometry methods, and peptide stability under various experimental conditions. These applications are essential for ensuring the reproducibility, scalability, and quality control of peptide production in research and industrial settings.
Functional studies of POMC derivatives: The C-terminal ACTH (18-39) segment is also investigated for its potential modulatory effects on biological processes independent of classical ACTH activity. Researchers explore its influence on peptide processing, intracellular trafficking, and possible interactions with non-classical binding partners. Such studies contribute to a broader understanding of POMC-derived peptide biology and may reveal novel regulatory mechanisms within neuroendocrine and metabolic pathways.
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