ACTH (34-39) is an adrenocorticotropic hormone fragment.
CAT No: R1157
CAS No:69454-10-0
Synonyms/Alias:ACTH (34-39);69454-10-0;AFPLEF-OH;(4S)-4-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-Aminopropanoyl]amino]-3-phenylpropanoyl]pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]-5-[[(1S)-1-carboxy-2-phenylethyl]amino]-5-oxopentanoic acid;ACTH 34-39;HY-P1739;DA-70571;FA108386;MS-31241;CS-0095089;G12209;H-Ala-Phe-Pro-Leu-Glu-Phe-OH; H-AFPLEF-OH;
ACTH 34-39, also known as C-terminal adrenocorticotropic hormone fragment (Arg-Lys-Val-Tyr-Pro), is a synthetic peptide corresponding to the amino acid residues 34 through 39 of the full-length ACTH molecule. As a short peptide segment derived from the larger ACTH sequence, it retains specific biochemical features relevant to peptide research and neuroendocrine studies. Its structure and sequence make it a valuable tool for dissecting the structure-activity relationships of ACTH and related peptides, as well as for exploring the roles of peptide fragments in cellular signaling and receptor interactions. Owing to its defined sequence and physicochemical properties, ACTH 34-39 is frequently utilized in laboratory investigations focused on peptide function, metabolism, and molecular recognition.
Peptide structure-function analysis: Researchers employ ACTH 34-39 to investigate the minimal structural motifs necessary for biological activity within the ACTH molecule. By comparing the activity of this C-terminal fragment to longer or full-length ACTH peptides, scientists can delineate the contribution of specific amino acid sequences to receptor binding, signaling pathways, or enzymatic processing. Such studies are crucial for understanding how peptide truncation or modification influences function, which in turn informs the design of novel analogs or inhibitors for further research.
Receptor binding studies: The defined sequence of the ACTH 34-39 fragment allows for precise assessment of its interaction with peptide receptors, particularly those implicated in the melanocortin system. By using radiolabeled or fluorescently tagged versions of this peptide, researchers can quantify binding affinities, map receptor subtypes, and elucidate the molecular determinants of ligand recognition. These experiments provide insight into the selectivity and specificity of peptide-receptor interactions, supporting the development of targeted probes or modulators for neuroendocrine research.
Peptide metabolism and degradation assays: ACTH 34-39 serves as a model substrate in studies of peptide stability, enzymatic cleavage, and metabolic fate. Enzymologists utilize this fragment to characterize the activity of peptidases and proteases that may process endogenous ACTH or related peptides in biological systems. Monitoring the degradation kinetics and identifying metabolic products contribute to a deeper understanding of peptide turnover, bioavailability, and regulatory mechanisms in peptide signaling pathways.
Immunological assay development: The unique C-terminal sequence of ACTH 34-39 can be harnessed as an immunogen or standard in the development and validation of peptide-specific antibodies. By generating and characterizing antibodies that recognize this fragment, researchers can improve the specificity of immunoassays aimed at detecting ACTH derivatives or monitoring peptide processing in vitro. This application is particularly relevant for studies requiring discrimination between intact hormone and its processed forms, enhancing the accuracy of biochemical analyses.
Peptide synthesis and analytical method validation: As a chemically well-defined peptide, ACTH 34-39 is frequently used as a reference compound in the optimization and validation of peptide synthesis protocols. Synthetic chemists utilize it to evaluate coupling efficiencies, purification strategies, and analytical detection methods such as HPLC or mass spectrometry. Employing this fragment as a standard supports quality control and method development in peptide production, ensuring reproducibility and reliability in peptide-based research workflows.
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