Katacalcin (PDN 21) is a potent plasma calcium-lowering peptide.
CAT No: R1464
CAS No:85916-47-8
Synonyms/Alias:Katacalcin;hCCAP;CCP I;Human ccap;Katacalcin (human);CCAP (katacalcin);85916-47-8;Pdn-21;Calcitonin carboxyl-terminal flanking peptide;Peptide (aspartic acid-asparagine);Calcitonin carboxyl-terminal peptide, human;CCP (calcitonin carboxyl-terminal peptide);Preprocalcitonin carboxyl-terminal region peptide;
Katacalcin is a peptide compound derived from the C-terminal region of the prohormone calcitonin, and is classified as a 21-amino acid peptide. As a naturally occurring regulatory peptide, it is co-secreted with calcitonin and calcitonin gene-related peptide (CGRP) from the parafollicular C-cells of the thyroid gland. Katacalcin's biochemical significance is underscored by its role in calcium and phosphate metabolism, as well as its emerging relevance in the study of peptide hormone processing and secretion. Its unique structural and functional properties make it a valuable tool for researchers investigating peptide hormone biosynthesis, endocrine signaling pathways, and the physiological regulation of mineral homeostasis.
Peptide hormone research: Katacalcin serves as an important model for studying the biosynthesis, processing, and secretion of peptide hormones within the endocrine system. Its close association with calcitonin and CGRP provides a unique opportunity to dissect the molecular mechanisms governing prohormone cleavage and the coordinated release of multiple bioactive peptides from a single precursor. By employing katacalcin in in vitro or ex vivo systems, researchers can elucidate the enzymatic pathways and regulatory controls that dictate peptide maturation and secretion dynamics, thereby advancing understanding of endocrine peptide biology.
Calcium and phosphate metabolism studies: The peptide's involvement in mineral homeostasis renders it a useful probe for exploring the physiological regulation of calcium and phosphate levels. Experimental use of katacalcin in cell-based assays or animal models enables detailed analysis of its effects on bone, kidney, and parathyroid function. Investigators can leverage its activity to investigate the interplay between various hormonal regulators of mineral metabolism, contributing to a more comprehensive understanding of systemic mineral balance and related pathophysiological conditions.
Receptor interaction analysis: Katacalcin is instrumental in delineating receptor-ligand interactions within the calcitonin peptide family. Its structural similarity to other family members allows for comparative studies of receptor binding affinities, signaling specificity, and downstream cellular responses. Utilizing synthetic or recombinant forms of the peptide, researchers can characterize receptor activation profiles, uncover novel signaling pathways, and evaluate the pharmacological properties of peptide-receptor interactions in diverse cellular contexts.
Peptide structure-function relationship investigations: The defined amino acid sequence and unique C-terminal origin of katacalcin make it a prime candidate for studies focused on peptide structure-activity relationships. Through systematic modification, labeling, or mutagenesis, researchers can identify critical residues responsible for biological activity, stability, or receptor engagement. Such studies not only enhance fundamental understanding of peptide function but also inform the rational design of novel peptide analogs with tailored biochemical properties.
Analytical method development: Due to its well-characterized sequence and physiological relevance, katacalcin is frequently employed as a reference standard or analytical target in the development and validation of peptide quantification methods. Techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays benefit from the use of this peptide for calibration, sensitivity assessment, and assay optimization. Its inclusion in analytical workflows supports accurate detection and quantification of peptide hormones in complex biological matrices, facilitating robust biochemical research and assay development.
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