Syntide 2 is recognized as a substrate by Ca2+/calmodulin-dependent protein kinase II (CaMKII) with a Ki of 12 μM.
CAT No: R1699
CAS No:108334-68-5
Synonyms/Alias:Syntide-2;108334-68-5;Pro-leu-ala-arg-thr-leu-ser-val-ala-gly-leu-pro-gly-lys-lys;DTXSID70148504;L-Lysine, L-prolyl-L-leucyl-L-alanyl-L-arginyl-L-threonyl-L-leucyl-L-seryl-L-valyl-L-alanylglycyl-L-leucyl-L-prolylglycyl-L-lysyl-;Syntide 2 trifluoroacetate salt;DTXCID5070995;EX-A10862;Syntide-2, Protein Kinase Substrate;FS110424;A11885;H-Pro-Leu-Ala-Arg-Thr-Leu-Ser-Val-Ala-Gly-Leu-Pro-Gly-Lys-Lys-OH; H-PLARTLSVAGLPGKK-OH;L-Lysine,L-prolyl-L-leucyl-L-alanyl-L-arginyl-L-threonyl-L-leucyl-L-seryl-L-valyl-L-alanylglycyl-L-leucyl-L-prolylglycyl-L-lysyl-;
Syntide 2 is a synthetic peptide substrate widely recognized in biochemical research for its utility in kinase assays and enzymatic activity studies. Comprising a defined amino acid sequence, this peptide is specifically engineered to serve as an optimal substrate for a range of serine/threonine kinases, including protein kinase A (PKA) and protein kinase C (PKC). Its well-characterized structure and predictable phosphorylation profile make it an invaluable tool for probing kinase function, dissecting signal transduction pathways, and supporting the development of high-throughput screening methodologies. The robust performance and reproducibility of Syntide 2 have established it as a standard reagent in both academic and industrial research settings focused on cellular signaling and enzyme kinetics.
Kinase substrate assays: Syntide 2 is extensively used as a model substrate in serine/threonine kinase assays, particularly for evaluating the activity of PKA, PKC, and related enzymes. The peptide's specific amino acid sequence enables efficient phosphorylation at the serine residue, facilitating quantitative measurement of kinase activity in vitro. Researchers employ it to determine enzyme kinetics, assess inhibitor potency, and compare substrate specificity across kinase families, thereby providing crucial insights into enzyme regulation and signal transduction mechanisms.
Signal transduction research: In the study of cellular signaling pathways, Syntide 2 serves as a reliable probe for monitoring kinase-mediated phosphorylation events. Its use allows researchers to dissect the functional roles of kinases within complex biological networks by offering a consistent and sensitive readout of enzymatic activity. The peptide's defined sequence and phosphorylation dynamics support mechanistic investigations into how extracellular stimuli or pharmacological agents modulate intracellular signaling cascades.
High-throughput screening: The reproducibility and robust phosphorylation characteristics of Syntide 2 make it an ideal choice for high-throughput screening platforms aimed at identifying kinase modulators. Biotechnological and pharmaceutical laboratories utilize this peptide in automated assay systems to screen large compound libraries for potential kinase inhibitors or activators. Its compatibility with radiometric, fluorescent, and colorimetric detection methods enhances assay versatility and data quality, streamlining the early stages of drug discovery and lead optimization.
Enzyme kinetics and mechanistic studies: Syntide 2 is frequently employed in detailed kinetic analyses to elucidate the catalytic properties of serine/threonine kinases. By providing a defined and consistent substrate, it enables accurate determination of kinetic parameters such as Km and Vmax, as well as mechanistic evaluation of enzyme-substrate interactions. These studies are fundamental for understanding the molecular basis of kinase catalysis, substrate recognition, and the impact of regulatory factors on enzymatic function.
Analytical method development: The peptide's predictable behavior in phosphorylation assays makes it a valuable standard for developing and validating analytical methods in enzymology and biochemistry. Syntide 2 supports the calibration of detection systems, optimization of assay conditions, and benchmarking of new methodologies for quantifying kinase activity. Its use in method development ensures consistency, reproducibility, and reliability across diverse research and industrial applications, contributing to the advancement of biochemical assay technology.
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