ACTH (22-39) is an adrenocorticotropic hormone (ACTH) fragment. ACTH (22-39) is the 22-39 sequence of ACTH.
CAT No: R1156
CAS No:37548-29-1
Synonyms/Alias:37548-29-1;22-39-ACTH (human);EX-A7455;MFCD00076176;FA108797;ACTH (22-39) (H-L-Val-L-Tyr-L-Pro-L-Asn-Gly-L-Ala-L-Glu-L-Asp-L-Glu-L-Ser-L-Ala-L-Glu-L-Ala-L-Phe-L-Pro-L-Leu-L-Glu-L-Phe-OH);H-Val-Tyr-Pro-Asn-Gly-Ala-Glu-Asp-Glu-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-OH; H-VYPNGAEDESAEAFPLEF-OH;
ACTH 22-39, also known as Adrenocorticotropic Hormone fragment 22-39, is a synthetic peptide corresponding to the C-terminal portion of the full-length ACTH molecule. As a truncated segment of the endogenous polypeptide hormone, it lacks the N-terminal region required for classical receptor-mediated adrenal stimulation, yet retains unique structural features that have attracted interest in biochemical and physiological research. Its distinct sequence enables selective investigation of non-steroidogenic functions, peptide-receptor interactions, and structure-activity relationships within the melanocortin family. ACTH 22-39 serves as a valuable tool for dissecting the functional domains of ACTH and understanding the broader signaling roles of pro-opiomelanocortin (POMC)-derived peptides.
Peptide structure-function analysis: ACTH 22-39 is widely employed in structure-activity relationship studies to delineate the functional domains of the parent ACTH molecule. By comparing the biological activity of this C-terminal fragment to that of the full-length hormone and other truncated analogs, researchers can map regions critical for receptor binding and biological responses. Such comparative assays provide insights into the minimal structural requirements for ACTH's diverse physiological effects, informing the rational design of peptide analogs with tailored bioactivity.
Receptor binding specificity: The absence of the N-terminal motif in ACTH 22-39 renders it inactive at the classical melanocortin 2 receptor (MC2R), which is responsible for adrenal steroidogenesis. However, this fragment is instrumental in probing the selectivity and binding affinity of other melanocortin receptors, such as MC3R and MC4R, as well as potential non-canonical binding partners. By using the peptide in competitive binding and displacement assays, investigators can characterize receptor-ligand interactions and uncover previously unrecognized signaling pathways modulated by ACTH-derived fragments.
Peptide metabolism and degradation studies: As a defined polypeptide fragment, ACTH 22-39 is routinely used to investigate the enzymatic degradation and metabolic fate of melanocortin peptides. Its susceptibility to proteolytic cleavage, as compared to intact ACTH, offers a model for studying the stability, half-life, and degradation pathways of peptide hormones in biological matrices. Such studies are essential for understanding peptide turnover, identifying bioactive metabolites, and optimizing peptide-based research tools.
Immunological assay standardization: The unique sequence of ACTH 22-39 makes it a useful calibrator or negative control in immunoassays designed to detect full-length ACTH or related peptides. Its inclusion in assay development allows for the assessment of antibody specificity, cross-reactivity, and the discrimination of structurally related peptide fragments. This application is particularly relevant for the validation of immunodiagnostic reagents and the refinement of quantitative peptide detection methods in complex biological samples.
Peptide synthesis and analytical method development: ACTH 22-39 serves as a reference standard in the optimization of solid-phase peptide synthesis protocols and analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its defined sequence and physicochemical properties provide a benchmark for evaluating peptide purity, chromatographic separation, and detection sensitivity. These methodological advances support the broader field of peptide chemistry and facilitate the reliable production and characterization of research-grade peptides.
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