(Ala13)-Apelin-13 (human, bovine, mouse, rat)

(Ala13)-Apelin-13 (human, bovine, mouse, rat) is a synthetic peptide analogue derived from the endogenous apelin-13 sequence, with an alanine substitution at the C-terminal position 13. As a member of the apelin peptide family, it is recognized for its role as a bioactive ligand of the G protein-coupled APJ receptor, which is involved in a diverse array of physiological processes across multiple mammalian species. The structural modification present in this analogue enables researchers to dissect the functional significance of the terminal residue in receptor interaction, signaling efficacy, and downstream biological effects. Its utility extends to comparative studies in human, bovine, mouse, and rat systems, providing a versatile platform for exploring conserved and species-specific aspects of apelinergic signaling.

Peptide receptor interaction studies: (Ala13)-Apelin-13 is widely employed in investigations focused on the molecular determinants of APJ receptor binding and activation. By substituting the terminal phenylalanine with alanine, researchers can elucidate the contribution of this residue to ligand-receptor affinity, signal transduction potency, and receptor selectivity. Such studies are essential for mapping the structure-activity relationships that govern peptide-receptor dynamics, thereby advancing the understanding of GPCR modulation by apelin analogues.

Signal transduction analysis: The altered peptide serves as a valuable molecular tool for dissecting intracellular signaling pathways initiated by APJ activation. Its use in cell-based assays allows for the assessment of second messenger generation, such as cyclic AMP or calcium mobilization, in response to modified ligand engagement. By comparing the signaling profiles of native and alanine-substituted apelin-13, researchers gain insights into the mechanisms underlying biased agonism, partial agonist activity, or receptor desensitization phenomena.

Comparative physiology research: Owing to its cross-species sequence compatibility, (Ala13)-Apelin-13 enables direct comparative studies in human, bovine, mouse, and rat models. This feature is particularly valuable for investigating evolutionary conservation and divergence in apelinergic system function. Researchers can employ the peptide to probe species-specific receptor pharmacology, tissue distribution, and physiological roles, facilitating translational insights and the identification of conserved regulatory mechanisms.

Peptide structure-activity relationship (SAR) studies: The alanine substitution at position 13 provides a strategic modification for systematic SAR investigations. By analyzing the effects of this single-residue change on biological activity, stability, and receptor interaction, scientists can delineate critical features required for optimal peptide function. Such SAR data are instrumental in guiding the rational design of novel apelin analogues with tailored properties for experimental applications.

Peptide synthesis validation and analytical calibration: As a well-characterized synthetic peptide, (Ala13)-Apelin-13 is frequently utilized as a reference standard in peptide synthesis workflows and analytical method development. Its defined sequence and physicochemical properties make it suitable for calibrating mass spectrometry, HPLC, and related analytical platforms. Employing the peptide as a control aids in validating peptide production processes, ensuring reproducibility, and benchmarking the performance of peptide quantification techniques.

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