Calcitonin, eel TFA

Calcitonin, eel TFA is the thyroid hormone peptide that contributes to the regulation of calcium homeostasis, widely used in the research of postmenopausal osteoporosis.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1265

Synonyms/Alias:Thyrocalcitonin eel (TFA)

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M.F/Formula
C₁₄₈H₂₄₂F₃N₄₃O₄₉S₂
M.W/Mr.
3528.89
Sequence
One Letter Code: CSNLSTCVLGKLSQELHKLQTYPRTDVGAGTP-NH2 (Disulfide bridge: Cys1-Cys7)
three Letter Code: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asp-Val-Gly-Ala-Gly-Thr-Pro-NH2 (Disulfide bridge: Cys1-Cys7)

Calcitonin, eel TFA is a peptide hormone derived from the eel species, commonly supplied as the trifluoroacetate (TFA) salt for enhanced stability and solubility. As a member of the calcitonin family, this peptide is structurally characterized by its 32-amino acid sequence and its distinct disulfide bridge, which are essential for its biological activity. Its primary function in vertebrates involves the regulation of calcium and phosphate metabolism, making it a valuable tool in studies of endocrine signaling, bone biology, and mineral homeostasis. The eel variant is particularly notable for its high potency and stability, traits that have contributed to its widespread use in comparative endocrinology and receptor pharmacology research. Beyond its physiological relevance, calcitonin peptides serve as important references in the design and evaluation of analogs with improved bioactivity or altered receptor specificity.

Receptor binding studies: Researchers frequently employ eel calcitonin in receptor binding assays to elucidate the molecular interactions between calcitonin peptides and their cognate G protein-coupled receptors. Its high affinity for calcitonin receptors makes it an ideal reference ligand for competitive binding experiments, enabling the characterization of receptor subtypes, mapping of ligand-binding domains, and comparison of species-specific pharmacological profiles. These investigations support the development of novel calcitonin analogs and provide insights into the structural determinants of receptor activation.

Signal transduction analysis: The peptide is extensively used to probe downstream signaling pathways triggered by calcitonin receptor activation. By applying eel calcitonin to cultured cells or tissue preparations, scientists can monitor cyclic AMP accumulation, intracellular calcium mobilization, and other second messenger responses. Such studies facilitate a deeper understanding of the mechanisms by which calcitonin modulates cellular physiology, and they help clarify the role of receptor desensitization, internalization, and cross-talk with related signaling systems.

Bone metabolism research: Due to its potent hypocalcemic effect in non-mammalian vertebrates, eel calcitonin serves as a valuable model compound for investigating the regulation of bone resorption and formation. Researchers utilize it to study osteoclast and osteoblast activity, assess the molecular pathways underlying bone mineralization, and explore the hormonal control of skeletal homeostasis. Its use in in vitro and ex vivo systems allows for precise dissection of the peptide's impact on bone cell function and the extracellular matrix.

Comparative endocrinology: Eel calcitonin provides a unique perspective for comparative studies across vertebrate species. Its structural differences from mammalian calcitonins enable researchers to explore evolutionary adaptations in peptide hormones and their receptors. These investigations inform the understanding of functional divergence, receptor specificity, and the conservation of hormonal signaling mechanisms. The peptide's robust activity profile makes it a preferred tool for cross-species analyses and evolutionary biology research.

Peptide analog development: The well-characterized sequence and pharmacological properties of eel calcitonin make it a reference standard in the design and screening of synthetic peptide analogs. Scientists leverage its structure as a template for engineering new molecules with enhanced receptor selectivity, improved metabolic stability, or altered signaling profiles. Such analogs are instrumental in dissecting structure-activity relationships and advancing the field of peptide-based research tools. By providing a benchmark for activity and stability, eel calcitonin supports the iterative optimization of next-generation peptide ligands.

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