Tyrosine Kinase Peptide 1 [KVEKIGEGTYGVVYK]

Product Name: Tyrosine Kinase Peptide 1 [KVEKIGEGTYGVVYK]

Sequence One Letter Code: KVEKIGEGTYGVVYK

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

Chemical Formula:C77H125N19O22

Molecular Weight: 1670

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: peptide substrate

Source / Species: Xenopus

Conjugation: Unconjugated

Code Nacres: NA.26

Application: Tyrosine Kinase Peptide 1 (KVEKIGEGTYGVVYK) is a synthetic substrate derived from residues 6–20 of CDC2/CDK1 and is widely used for evaluating tyrosine protein kinase activity. The central tyrosine residue serves as the phosphorylation site, enabling quantitative analysis of kinase-mediated phosphotransfer. This peptide is compatible with radiometric, colorimetric, and fluorescence-based detection platforms and is broadly applied in kinase profiling, enzymatic characterization, and inhibitor screening to investigate phosphorylation-dependent signaling mechanisms.

Current Research: Tyrosine Kinase Peptide 1 (KVEKIGEGTYGVVYK) is a synthetic phosphorylation substrate derived from residues 6–20 of CDC2/CDK1, engineered for quantitative assessment of protein tyrosine kinase activity. The sequence contains a centrally positioned tyrosine residue, which serves as the phospho-acceptor site for kinase-mediated transfer of the γ-phosphate group from ATP. Because of its defined structure, solubility, and reproducible phosphorylation characteristics, this peptide is widely used as a general-purpose substrate in kinase activity assays, enzymatic profiling, and inhibitor screening platforms. Structural and Functional Features The peptide sequence: KVEKIGEGTYGVVYK includes: A single, accessible tyrosine residue for phosphorylation Flanking residues that support efficient recognition by multiple tyrosine kinases Terminal lysine residues enhancing solubility and compatibility with assay systems Phosphorylation of the central tyrosine introduces a negative charge and alters peptide mass, enabling detection by multiple analytical methods. Applications in Kinase Research 1. Radiometric Assays The peptide is compatible with γ-³²P-ATP–based assays, where incorporation of radioactive phosphate into the tyrosine residue provides highly sensitive quantification of kinase activity. 2. Colorimetric and ELISA-Based Platforms Following phosphorylation, the peptide can be detected using anti-phosphotyrosine antibodies in ELISA or plate-based immunoassays, enabling non-radioactive quantification. 3. Fluorescence-Based Detection Phosphorylation-dependent fluorescence assays or coupled detection systems can be employed for real-time or endpoint measurements in microplate formats. 4. Mass Spectrometry Analysis The defined mass shift upon phosphorylation allows direct verification and quantification using LC–MS–based workflows. Research Applications Kinase profiling across multiple tyrosine kinase families Determination of kinetic parameters (Km, Vmax) Comparative activity analysis of wild-type and mutant kinases Inhibitor screening and IC₅₀ determination Mechanistic investigation of phosphorylation-dependent signaling pathways The substrate is particularly useful in evaluating receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases under standardized assay conditions. Advantages Defined single phosphorylation site High solubility and stability Broad compatibility with detection platforms Suitable for high-throughput screening Reproducible performance across assay formats Experimental Considerations Optimal substrate concentration should be selected relative to the kinase’s Km to ensure accurate kinetic analysis. ATP concentration and magnesium ion availability are critical for enzymatic activity. Inclusion of appropriate controls, including kinase inhibitors or inactive enzyme variants, is recommended to confirm specificity.