Calcineurin substrate is a peptide from the regulatory RII subunit of cAMP-dependent protein kinase. It can be used in the calcineurin activity assay.
CAT No: R1259
CAS No:113873-67-9
Synonyms/Alias:Calcineurin substrate;113873-67-9;L-Glutamic acid, L-alpha-aspartyl-L-leucyl-L-alpha-aspartyl-L-valyl-L-prolyl-L-isoleucyl-L-prolylglycyl-L-arginyl-L-phenylalanyl-L-alpha-aspartyl-L-arginyl-L-arginyl-L-valyl-L-seryl-L-valyl-L-alanyl-L-alanyl-;CALCINEURIN SUBSTRATE TRIFLUOROACETATE SALT;DTXSID20583284;AS-79963;DA-51536;FC108597;PD150550;G90964;Calcineurin Substrate trifluoroacetate salt H-Asp-Leu-Asp-Val-Pro-Ile-Pro-Gly-Arg-Phe-Asp-Arg-Arg-Val-Ser-Val-Ala-Ala-Glu-OH trifluo roacetate salt;L-alpha-Aspartyl-L-leucyl-L-alpha-aspartyl-L-valyl-L-prolyl-L-isoleucyl-L-prolylglycyl-L-arginyl-L-phenylalanyl-L-alpha-aspartyl-L-arginyl-L-arginyl-L-valyl-L-seryl-L-valyl-L-alanyl-L-alanyl-L-glutamic acid;
Calcineurin substrate is a specialized biochemical reagent widely utilized in the study of protein phosphatases, particularly within the context of calcium-dependent signal transduction pathways. As a synthetic or natural peptide or protein sequence recognized and dephosphorylated by the enzyme calcineurin (protein phosphatase 2B), it serves as a critical tool in elucidating the molecular mechanisms underlying cellular responses to calcium signaling. The unique ability of calcineurin to specifically dephosphorylate serine or threonine residues in target substrates makes this compound indispensable for researchers investigating the regulation of diverse physiological processes, including neuronal activity, immune cell function, and muscle contraction. Its selective interaction with calcineurin allows for precise assessment of phosphatase activity in vitro, facilitating advanced research into the modulation and dynamics of signal transduction networks.
Enzyme activity assays: In biochemical research, calcineurin substrate is routinely employed as a reporter molecule in quantitative phosphatase activity assays. By providing a defined phosphorylation site that is specifically recognized by calcineurin, the substrate enables researchers to directly measure enzymatic activity through the detection of released phosphate or changes in substrate conformation. This approach is fundamental for characterizing the kinetic properties of calcineurin, evaluating the specificity of enzyme-substrate interactions, and screening for modulators or inhibitors that may influence phosphatase function. The use of such substrates ensures high assay sensitivity and selectivity, thereby supporting robust and reproducible experimental outcomes.
Signal transduction studies: The substrate plays a pivotal role in dissecting calcium-dependent signaling pathways, particularly those mediated by calcineurin in neuronal and immune cell contexts. By serving as a molecular probe, it allows for the investigation of downstream dephosphorylation events following calcium influx and calmodulin activation. This utility is essential for mapping the sequence of events that lead to transcription factor activation, gene expression changes, or alterations in cellular phenotype. Researchers leverage these substrates to clarify the role of calcineurin in synaptic plasticity, T-cell activation, and other calcium-regulated processes, thereby expanding our understanding of cellular communication networks.
Inhibitor screening and drug discovery: The use of calcineurin substrate is integral to high-throughput screening platforms designed to identify and characterize small molecule inhibitors or modulators of calcineurin activity. By monitoring the dephosphorylation of the substrate in the presence of candidate compounds, researchers can rapidly assess inhibitory potency and selectivity. This application supports the development of novel research tools and chemical probes, as well as the exploration of pathways that may be therapeutically relevant in immunology, neurobiology, and related fields. The substrate's defined reactivity profile ensures reliable differentiation between specific and off-target effects during compound evaluation.
Protein engineering and mutagenesis research: Investigators studying the structure-function relationships of calcineurin or its substrates frequently utilize defined peptide or protein substrates to assess the impact of amino acid substitutions, domain deletions, or post-translational modifications on enzyme recognition and catalysis. By systematically varying substrate sequences and analyzing dephosphorylation efficiency, researchers gain mechanistic insights into substrate specificity determinants, allosteric regulation, and the molecular basis for disease-associated mutations. These findings inform the rational design of engineered proteins and synthetic substrates with tailored properties for advanced biochemical studies.
Analytical method development: Calcineurin substrates are also employed in the optimization and validation of analytical techniques for phosphatase detection, including spectrophotometric, fluorometric, and mass spectrometry-based assays. By providing a well-characterized target for enzymatic dephosphorylation, these substrates facilitate the calibration of assay sensitivity, dynamic range, and reproducibility. Their use enhances the reliability of quantitative measurements in complex biological samples, supporting the advancement of experimental protocols in both basic and applied research laboratories.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More