Myelin Basic Protein (95-98) S5 Peptide MAP Kinase Substrate TFA contains a short motif tailored for phosphorylation studies. Its basic and polar residues influence kinase accessibility and secondary-structure tendencies. Researchers utilize it to examine catalytic specificity and charge-dependent interactions. Applications span signaling-pathway mapping, substrate profiling, and structural biochemistry.
CAT No: R2337
CAS No:138028-00-9
Synonyms/Alias:Myelin Basic Protein (95-98) S5 Peptide MAP Kinase Substrate Trifluoroacetate;138028-00-9;Myelin Basic Protein (95-98) S5 Peptide MAP Kinase Substrate Trifluoroacetate;(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-aminopropanoyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]acetyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid;2,2,2-trifluoroacetic acid;H-Ala-Pro-Arg-Thr-Pro-Gly-Gly-Arg-Arg-OH;FA108939;
Myelin Basic Protein (95-98) S5 Peptide MAP Kinase Substrate Trifluoroacetate is a specialized synthetic peptide fragment derived from the myelin basic protein sequence, specifically encompassing amino acids 95 to 98. This peptide is meticulously engineered to serve as a substrate for mitogen-activated protein (MAP) kinase assays, making it a valuable research tool in signal transduction studies. The addition of trifluoroacetate as a counterion enhances its solubility and stability, facilitating ease of use in various biochemical and molecular biology applications. As a highly specific substrate, it enables precise monitoring of kinase activity, thus supporting a broad spectrum of experimental approaches in cellular signaling research. The peptide's design ensures minimal interference from extraneous sequences, allowing for accurate assessment of kinase-substrate interactions and downstream phosphorylation events.
Protein Phosphorylation Studies: Myelin Basic Protein (95-98) S5 Peptide MAP Kinase Substrate Trifluoroacetate is widely utilized in phosphorylation assays to investigate the activity of MAP kinases and related enzymes. By providing a defined substrate, researchers can quantify phosphorylation rates, compare kinase activities across experimental conditions, and elucidate the regulatory mechanisms governing signal transduction pathways. Its clear sequence specificity allows for reproducible results, which are critical for dissecting the roles of kinases in cellular processes such as proliferation, differentiation, and stress responses. The peptide is often incorporated into in vitro kinase assays, enabling the detection of phosphorylation events via radiolabeling, mass spectrometry, or antibody-based techniques.
Enzyme Kinetics Research: The MBP (95-98) S5 peptide serves as an ideal model substrate for kinetic analyses of MAP kinases and related signaling enzymes. Researchers can use it to determine kinetic parameters such as Km and Vmax, offering insights into enzyme efficiency and substrate affinity. By evaluating how different inhibitors or activators affect kinase activity in the presence of this peptide, scientists can better understand the regulatory dynamics of key signaling pathways. The reproducibility and specificity of the substrate streamline the study of enzyme-substrate interactions, making it indispensable for fundamental and applied research in enzymology.
Cell Signaling Pathway Elucidation: Utilizing the myelin basic protein-derived peptide enables the mapping of MAP kinase signaling cascades within various biological systems. By tracking phosphorylation events mediated by MAP kinases, scientists can delineate the sequence of molecular events following extracellular stimuli. The peptide's compatibility with a range of detection methods, including electrophoresis and immunoblotting, supports detailed analysis of pathway activation and cross-talk between signaling modules. These studies contribute to a deeper understanding of how cells respond to growth factors, cytokines, and environmental stressors.
Inhibitor Screening Assays: The MBP (95-98) S5 peptide is frequently employed in high-throughput screening platforms designed to identify novel modulators of MAP kinase activity. Its defined structure and phosphorylation sites make it an excellent reporter for detecting changes in kinase activity in response to small molecules, peptides, or genetic perturbations. The peptide enables rapid and sensitive assessment of compound efficacy, facilitating the discovery of potential therapeutic agents targeting dysregulated kinase signaling in various disease models. The use of this substrate also minimizes background noise and enhances the reliability of assay readouts.
Biochemical Method Development: Researchers leverage the myelin basic protein (95-98) S5 peptide in the optimization and validation of new analytical techniques for studying protein phosphorylation. Its consistent performance across multiple assay formats makes it a standard substrate for calibrating detection systems, benchmarking assay sensitivity, and troubleshooting experimental protocols. The peptide's versatility supports its integration into emerging technologies such as multiplexed kinase assays and real-time phosphorylation monitoring, driving innovation in biochemical and molecular biology research. As a result, it remains a cornerstone reagent in laboratories dedicated to unraveling the complexities of protein phosphorylation and MAP kinase signaling.
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