(Ala13)-Apelin-13 (human, bovine, mouse, rat) incorporates a targeted alanine substitution that alters backbone conformation and receptor-binding determinants. Researchers study its folding and hydrogen-bond networks to assess structural impact. Its sequence supports motif-function exploration. Applications include peptide analog design, structural mapping, and ligand characterization.
CAT No: R2493
CAS No:568565-11-7
Synonyms/Alias:(Ala13)-Apelin-13;568565-11-7;(Ala13)-Apelin-13 (human, bovine, mouse, rat);[Ala13]-Apelin-13 trifluoroacetate salt;H-GLN-ARG-PRO-ARG-LEU-SER-HIS-LYS-GLY-PRO-MET-PRO-ALA-OH;H-Gln-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Ala-OH; H-QRPRLSHKGPMPA-OH;HY-P3162;TXA56511;AKOS040754605;CS-0166698;Gln-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Ala;NH2-Gln-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Ala-OH;
(Ala13)-Apelin-13 (human, bovine, mouse, rat) is a synthetic peptide analog designed to mimic the native apelin-13 sequence with a single amino acid substitution at the thirteenth position, where alanine replaces the original residue. This modification imparts unique biochemical characteristics, rendering the peptide a valuable tool for elucidating the structure-activity relationships within the apelinergic system. As a highly conserved ligand across multiple species, including human, bovine, mouse, and rat, (Ala13)-Apelin-13 enables comparative studies that bridge basic and translational research. Its stability and affinity for the apelin receptor (APJ) make it particularly suited for probing receptor-ligand interactions and downstream signaling pathways in a controlled laboratory setting. Researchers benefit from its versatility, as the peptide can be incorporated into a wide range of in vitro and in vivo experimental designs, supporting investigations into cardiovascular, metabolic, and neurobiological processes.
Receptor Binding Studies: In receptor binding assays, (Ala13)-Apelin-13 serves as a critical probe for delineating the molecular determinants of APJ receptor activation and ligand specificity. By substituting alanine at the thirteenth position, scientists can assess how this alteration impacts receptor affinity and signal transduction compared to the native apelin-13. Such studies are instrumental in mapping the pharmacophore of the apelinergic system, facilitating the rational design of novel agonists or antagonists with tailored functional profiles. The ability to utilize this analog in multiple species further enhances its utility in comparative pharmacology, enabling the identification of conserved and divergent features of APJ receptor engagement.
Cell Signaling Pathway Analysis: Utilizing the peptide in cellular models allows for precise interrogation of downstream signaling cascades initiated by APJ activation. (Ala13)-Apelin-13 is frequently employed to stimulate cells expressing the apelin receptor, permitting the quantification of second messenger production, kinase phosphorylation, and gene expression changes. These experiments yield insights into the functional consequences of receptor modulation and the role of specific amino acid residues in signal propagation. The analog's distinctive properties make it an invaluable tool for dissecting the molecular mechanisms underlying apelin-mediated effects in diverse cell types, including endothelial, neuronal, and adipocyte populations.
Cardiovascular Research: In the context of cardiovascular biology, the peptide analog is widely adopted to explore the apelinergic system's influence on cardiac function and vascular tone. Experimental models leveraging (Ala13)-Apelin-13 enable researchers to investigate how modifications at the peptide's C-terminus affect its ability to modulate contractility, vasodilation, and endothelial signaling. Such studies contribute to a deeper understanding of the peptide's role in maintaining cardiovascular homeostasis and provide a foundation for the development of targeted therapeutics aimed at modulating APJ activity in disease models.
Metabolic Regulation Studies: The application of (Ala13)-Apelin-13 extends to metabolic research, where it is used to examine the peptide's impact on glucose uptake, lipid metabolism, and energy expenditure. By comparing the biological activity of the alanine-substituted analog with that of native apelin-13, investigators can pinpoint structural features critical for metabolic regulation. These findings inform the design of peptide-based modulators with potential utility in managing metabolic dysfunctions and contribute to the broader understanding of peptide hormone action in energy balance.
Neurobiological Investigations: In neurobiology, the analog is utilized to probe the apelinergic system's involvement in neural signaling, synaptic plasticity, and neuroprotection. Experimental paradigms incorporating (Ala13)-Apelin-13 facilitate the assessment of how specific sequence modifications influence peptide-receptor interactions within the central nervous system. This approach aids in unraveling the complex roles played by apelin peptides in neural development and function, supporting the identification of novel molecular targets for further study.
Peptide Engineering and Drug Discovery: Beyond its established research applications, (Ala13)-Apelin-13 is a valuable scaffold in peptide engineering initiatives aimed at optimizing ligand-receptor interactions and enhancing peptide stability. The analog is frequently used as a reference compound in high-throughput screening platforms designed to identify new APJ modulators with improved pharmacological profiles. By serving as a benchmark for structure-activity relationship analyses, it accelerates the iterative process of lead optimization and supports the advancement of next-generation peptide therapeutics. Through these diverse applications, (Ala13)-Apelin-13 (human, bovine, mouse, rat) remains an indispensable resource for advancing our understanding of the apelinergic system across multiple biological disciplines.
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