CALP3 is a cell-permeable calmodulin (CaM) agonist that binds to the EF-hand/Ca2+-binding site. Activates phosphodiesterase in the absence of Ca2+ and inhibits Ca2+-mediated cytotoxicity and apoptosis (IC50 = 33 μM).
CAT No: 10-101-306
CAS No:261969-05-5
Synonyms/Alias:CALP3;261969-05-5;(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-amino-3-methylbutanoyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]hexanoic acid;VKFGVGFK;CALP3 TFA;CALP-3;HY-P1075;AKOS024457051;DA-71886;FC110060;MS-31632;Calcium-Like Peptide 3 trifluoroacetate salt;CS-0027558;G13351;H-Val-Lys-Phe-Gly-Val-Gly-Phe-Lys-OH; H-VKFGVGFK-OH;
Chemical Name:(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-amino-3-methylbutanoyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]hexanoic acid
CALP3 is a carbohydrate compound recognized for its unique structural properties and versatile reactivity, making it an invaluable tool in a variety of biochemical and analytical research settings. As a synthetic oligosaccharide, CALP3 offers well-defined molecular architecture that facilitates its integration into complex experimental designs. Its stability under diverse laboratory conditions and compatibility with a wide range of detection methods allow researchers to employ it in both qualitative and quantitative assays. The compound's ability to interact specifically with carbohydrate-binding proteins and enzymes adds further value, supporting investigations into glycan recognition, signal transduction, and molecular diagnostics. By leveraging these features, scientists are able to advance their understanding of carbohydrate-mediated biological processes and develop innovative methodologies for glycoscience research.
Glycan-Protein Interaction Analysis: CALP3 serves as a precise probe for studying glycan-protein interactions, enabling researchers to dissect the molecular mechanisms underlying carbohydrate recognition by lectins, antibodies, and other glycan-binding proteins. By incorporating CALP3 into microarray platforms or solution-based binding assays, investigators can evaluate binding affinities, specificities, and kinetics, thereby elucidating the structural requirements for selective recognition. This application is particularly valuable for identifying novel glycan-binding motifs and characterizing the functional roles of carbohydrates in cell signaling, immune modulation, and pathogen recognition.
Enzyme Substrate in Glycosylation Studies: As a structurally defined oligosaccharide, CALP3 is frequently utilized as a substrate in enzymatic assays to investigate the activity and specificity of glycosyltransferases, glycosidases, and other carbohydrate-active enzymes. Researchers can monitor the enzymatic modification of CALP3 using chromatographic or spectroscopic techniques, gaining insights into enzyme mechanisms, substrate preferences, and potential inhibitors. These studies contribute to a deeper understanding of glycan biosynthesis and degradation pathways, supporting the development of enzyme-targeted research tools and biotechnological applications.
Analytical Standard for Chromatography: CALP3's well-characterized structure makes it an ideal analytical standard for chromatographic techniques such as high-performance liquid chromatography (HPLC) and capillary electrophoresis. Laboratories employ it to calibrate instruments, validate separation methods, and ensure the accuracy of glycan profiling experiments. By providing a consistent reference point, CALP3 enhances the reliability of quantitative analyses and facilitates the comparison of results across different research groups or experimental conditions.
Biomarker Discovery and Validation: The specificity of CALP3 interactions with carbohydrate-binding proteins enables its use in biomarker discovery efforts. Researchers can utilize it to screen for disease-associated lectins or antibodies in biological samples, supporting the identification and validation of glycan-based biomarkers. This approach aids in unraveling the complex roles of carbohydrates in disease states and offers a foundation for the development of diagnostic assays and targeted research reagents.
Cell Surface Glycan Mapping: In cell biology and immunology research, CALP3 is employed to map the distribution and abundance of specific glycan structures on cell surfaces. By conjugating the compound to fluorescent or affinity tags, scientists can visualize and quantify its binding to target cells using flow cytometry or microscopy. Such studies provide critical insights into cell-cell communication, immune recognition, and the dynamic remodeling of cell surface glycans during development, differentiation, or disease progression.
Synthetic Biology and Glycoengineering: CALP3 is increasingly integrated into synthetic biology workflows aimed at designing and constructing novel glycan structures for research or biotechnological purposes. Its defined composition and reactivity enable precise control over glycan assembly, facilitating the engineering of glycoproteins, glycomaterials, or cell surfaces with tailored carbohydrate motifs. Through these applications, CALP3 empowers researchers to explore the functional consequences of glycan modification, develop innovative glycan-based tools, and advance the frontiers of glycoscience.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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