Tyrosine Kinase Peptide 1 [KVEKIGEGTYGVVYK], 5-TMR labeled

Product Name: Tyrosine Kinase Peptide 1 [KVEKIGEGTYGVVYK], 5-TMR labeled

Sequence One Letter Code: 5-TMR-KVEKIGEGTYGVVYK

Sequence Three Letter Code: 5-TMR-Lys-Val-Glu-Lys-Ile-Gly-Glu-Gly-Thr-Tyr-Gly-Val-Val-Tyr-Lys-OH

Chemical Formula:C106H148ClN21O29

Molecular Weight: 2082.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C Protected from light

Research Area: peptide substrate

Source / Species: Xenopus

Conjugation: Conjugated

Conjugation Type: Fluorescent dyes

Code Nacres: NA.26

Application: Tyrosine Kinase Peptide 1, 5-TMR labeled, is a fluorescent synthetic peptide substrate with the sequence KVEKIGEGTYGVVYK, derived from residues 6–20 of CDC2/CDK1. It functions as a generic substrate for tyrosine protein kinases (TPKs), enabling broad assessment of kinase activity across multiple enzyme families. The centrally positioned tyrosine residue serves as the phosphorylation site, supporting efficient catalytic turnover in biochemical assays. Conjugation with the 5-carboxytetramethylrhodamine (5-TMR) fluorophore permits fluorescence-based detection and quantitative analysis of phosphorylation events. This labeling strategy enables real-time monitoring and compatibility with high-throughput screening platforms. The peptide is widely used for kinase profiling, kinetic parameter determination, and inhibitor evaluation. By facilitating measurement of tyrosine phosphorylation dynamics, this substrate supports mechanistic studies of signal transduction pathways, oncogenic kinase activation, and the development of targeted tyrosine kinase inhibitors in cancer and cell signaling research.

Current Research: Tyrosine Kinase Peptide 1, 5-TMR labeled, is a fluorescent synthetic peptide substrate designed for broad evaluation of tyrosine protein kinase (TPK) activity. The peptide sequence, KVEKIGEGTYGVVYK, is derived from residues 6–20 of CDC2/CDK1 and contains a centrally positioned tyrosine residue that serves as the phosphorylation site. This configuration supports efficient catalytic turnover and reliable signal generation in biochemical kinase assays, making it a versatile tool for profiling diverse tyrosine kinases. Protein tyrosine phosphorylation is a central regulatory mechanism in cell signaling, controlling pathways involved in proliferation, differentiation, migration, immune activation, and apoptosis. Dysregulation of tyrosine kinase activity is strongly associated with oncogenesis, inflammatory disorders, and other pathological conditions. As research increasingly focuses on mapping kinase signaling networks and identifying selective inhibitors, robust and adaptable substrate systems are essential for accurate activity measurement. Tyrosine Kinase Peptide 1 fulfills this need by functioning as a generic substrate compatible with multiple tyrosine kinase families. The inclusion of the 5-carboxytetramethylrhodamine (5-TMR) fluorophore enables fluorescence-based detection of phosphorylation events. 5-TMR is a bright, photostable fluorophore with excitation and emission properties suitable for standard fluorescence detection systems. Labeling the peptide allows direct monitoring of kinase activity in real time or endpoint formats without the need for radioactive reagents. This supports safer laboratory workflows while maintaining high sensitivity and quantitative precision. In practical applications, phosphorylation of the tyrosine residue can be detected through fluorescence polarization, fluorescence resonance energy transfer (FRET)-based approaches, or antibody-coupled detection strategies. These formats allow measurement of kinase activity in purified enzyme systems, cell lysates, or reconstituted signaling complexes. The fluorescent tag enhances compatibility with automated plate readers and high-throughput screening platforms, making the peptide particularly valuable in drug discovery environments. Kinetic characterization represents a key use case for this substrate. By varying substrate or ATP concentrations, researchers can determine kinetic parameters such as Km and Vmax, providing insight into catalytic efficiency and enzyme–substrate affinity. These analyses support mechanistic studies of kinase regulation, including evaluation of activation loop phosphorylation, conformational changes, or mutation-driven alterations in activity. Because the peptide is structurally defined and reproducible, it enables consistent comparisons across experimental conditions. Tyrosine Kinase Peptide 1, 5-TMR labeled, is also widely applied in inhibitor screening and profiling campaigns. The robust fluorescence readout provides a reliable assay window for detecting competitive or allosteric inhibition. This is particularly relevant in oncology research, where aberrant activation of receptor and non-receptor tyrosine kinases drives tumor growth and metastasis. Screening candidate compounds against fluorescent peptide substrates helps identify molecules that effectively suppress kinase activity and guides subsequent structure–activity relationship optimization. Beyond oncology, the peptide supports broader investigations into signal transduction dynamics. Tyrosine phosphorylation events regulate receptor signaling cascades, cytoskeletal organization, and immune cell activation. By facilitating quantitative measurement of phosphorylation kinetics, this substrate contributes to mapping pathway activation profiles and understanding cross-talk between signaling networks. Overall, Tyrosine Kinase Peptide 1, 5-TMR labeled, provides a sensitive and adaptable platform for analyzing tyrosine kinase activity. Its well-defined phosphorylation site, compatibility with fluorescence-based detection, and suitability for kinetic and high-throughput applications make it a valuable reagent for mechanistic studies and therapeutic development. Through accurate assessment of tyrosine phosphorylation dynamics, this peptide supports ongoing research into cell signaling regulation and targeted kinase inhibitor discovery.