Calcitonin eel is a peptide hormone produced by the parafollicular C cells of the thyroid or by the ultimobranchial bodies of nonmammalian vertebrates.
CAT No: 10-101-218
CAS No:57014-02-5
Synonyms/Alias:Calcitonin (eel);Eel calcitonin;57014-02-5;Calcitonin, Eel;Eel Thyrocalcitonin;UNII-R5527T0R0U;HC 58;R5527T0R0U;MFCD00133858;G77957;
Calcitonin eel is a peptide hormone derived from the ultimobranchial glands of the eel species Anguilla japonica. Structurally, it is a 32-amino acid polypeptide notable for its high sequence homology to human calcitonin but with distinct differences that confer unique biological activity. As a member of the calcitonin family, this peptide is recognized for its potent ability to regulate calcium and phosphate metabolism in vertebrates. Its robust activity profile and evolutionary divergence from mammalian calcitonins make it a valuable tool in comparative endocrinology, receptor pharmacology, and bone metabolism research.
Peptide hormone research: As a model peptide hormone, eel calcitonin is extensively utilized to study the mechanisms of calcium homeostasis and bone remodeling. Its strong affinity for vertebrate calcitonin receptors allows researchers to probe the signal transduction pathways activated upon receptor binding, facilitating a deeper understanding of the molecular events governing mineral metabolism. The comparative analysis of eel and mammalian calcitonins provides insights into evolutionary adaptations in calcium regulatory systems across species.
Receptor binding and pharmacological profiling: Eel calcitonin serves as a reference ligand in receptor binding assays, enabling the characterization of calcitonin receptor subtypes and their pharmacological properties. Its high potency and stability make it particularly suitable for in vitro studies aimed at elucidating ligand-receptor interactions, receptor activation kinetics, and downstream signaling cascades. Such research is instrumental in the development of novel calcitonin analogs and receptor modulators for investigative purposes.
Peptide structure-function analysis: The unique amino acid sequence of eel calcitonin offers a valuable framework for structure-activity relationship (SAR) studies. By employing synthetic modifications or alanine-scanning mutagenesis, researchers can identify critical residues responsible for receptor binding and biological activity. These studies not only advance fundamental knowledge of peptide hormone function but also inform the rational design of peptide-based probes and research tools.
Biochemical assay development: Eel calcitonin is frequently incorporated into biochemical assays designed to measure calcitonin activity, receptor occupancy, or downstream effector responses. Its well-characterized activity profile allows for the calibration and validation of assay platforms in both academic and industrial research settings. The peptide's stability and reproducibility support its use as a standard or positive control in various in vitro testing formats, enhancing the reliability of experimental outcomes.
Comparative endocrinology: The study of eel calcitonin in non-mammalian systems provides a broader perspective on the evolution of peptide hormone function. Researchers utilize the peptide to investigate species-specific differences in hormone-receptor interactions, tissue distribution, and physiological effects. These comparative studies are essential for elucidating the adaptive significance of calcitonin signaling pathways and for identifying conserved versus divergent features among vertebrates.
Through these diverse applications, eel calcitonin stands as an essential reagent in peptide hormone research, receptor pharmacology, and biochemical assay development. Its unique properties continue to drive advancements in our understanding of calcium regulation and peptide structure-function relationships, supporting both basic and applied scientific investigations.
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