ACTH (1-39), PORCINE corresponds to the full porcine adrenocorticotropic hormone sequence, preserving motifs central to peptide folding and receptor engagement. The peptide enables studies of biosynthesis, structural transitions, and enzymatic cleavage. Researchers apply it to examine cross-species differences in ACTH behavior. Its extended length supports biophysical and biochemical investigations.
CAT No: HB00091
CAS No:9061-27-2
Synonyms/Alias:alpha1-39-Corticotropin (pig);9061-27-2;Corticotropin porcine;EINECS 232-946-7;UNII-FP33F50XKB;FP33F50XKB;CHEMBL3274100;232-946-7;
ACTH (1-39), PORCINE is a biologically active peptide corresponding to the full-length adrenocorticotropic hormone sequence derived from porcine sources. As a critical regulator within the hypothalamic-pituitary-adrenal (HPA) axis, this 39-amino acid peptide plays a central role in stimulating the adrenal cortex to produce glucocorticoids, mineralocorticoids, and androgens. Its structural and functional conservation across mammalian species has made it a valuable tool for investigating endocrine signaling, peptide-receptor interactions, and downstream metabolic pathways. The porcine variant is particularly relevant for comparative physiology studies due to its high homology with human and other mammalian ACTH, supporting its widespread use in biochemical, pharmacological, and molecular research contexts.
Endocrine signaling research: In fundamental studies of the HPA axis, the peptide is widely used to probe the mechanisms of pituitary-adrenal communication. Researchers employ ACTH (1-39), PORCINE in in vitro and ex vivo systems to stimulate adrenal cells or tissue explants, enabling the analysis of steroidogenic responses and the elucidation of signaling cascades triggered by ACTH receptor activation. These experiments are essential for dissecting the regulation of steroid biosynthesis, feedback inhibition, and the modulation of stress-responsive pathways at the molecular and cellular levels.
Peptide-receptor interaction studies: The full-length porcine ACTH is a preferred ligand in receptor binding assays and functional characterization of melanocortin 2 receptors (MC2R) and related G protein-coupled receptors. By applying this peptide to transfected cell lines or membrane preparations expressing MC2R, scientists can quantify binding affinities, assess receptor activation, and investigate the specificity and kinetics of peptide-receptor engagement. Such studies provide crucial insights into receptor pharmacology, ligand selectivity, and the structural determinants of peptide hormone action.
Comparative physiology and evolutionary biology: The conserved sequence and biological activity of ACTH (1-39), PORCINE make it an excellent model for cross-species analyses of pituitary-adrenal function. Its use in comparative studies facilitates the examination of evolutionary adaptations in hormone signaling, receptor evolution, and interspecies differences in stress response mechanisms. This approach aids in understanding both conserved and divergent aspects of endocrine regulation across vertebrate taxa.
Peptide synthesis and analytical standards: As a well-characterized, naturally occurring peptide, ACTH (1-39), PORCINE serves as a reference standard in peptide synthesis workflows and analytical method development. It is frequently utilized for validating chromatographic techniques such as HPLC and mass spectrometry, supporting accurate identification, quantification, and purity assessment of synthetic peptides. Its defined sequence and established physicochemical properties make it an ideal control for optimizing peptide purification and detection protocols.
Signal transduction and downstream effect studies: The peptide is instrumental in dissecting the intracellular signaling pathways activated upon ACTH stimulation. By applying it to various cell models, researchers can monitor downstream events such as cyclic AMP production, protein kinase A activation, and gene expression changes associated with steroidogenesis. These investigations help clarify the molecular mechanisms by which ACTH regulates adrenal function and contribute to the broader understanding of peptide hormone signaling networks in mammalian systems.
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