Date published: 2026-5-25

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Cdk2 Substrates

Santa Cruz Biotechnology now offers a broad range of Cdk2 Substrates for use in various applications. Cdk2, or Cyclin-Dependent Kinase 2, is a crucial enzyme in the regulation of the cell cycle, particularly in the progression through the S phase and the initiation of DNA replication. Cdk2 Substrates are vital tools in scientific research, allowing for the detailed investigation of Cdk2's role in cell cycle control and its interactions with various regulatory proteins. By using these substrates, researchers can study the specific phosphorylation events mediated by Cdk2, which are essential for understanding how cells regulate their growth and division under normal and stressed conditions. These substrates are commonly employed in in vitro kinase assays, where they provide insights into the enzyme's activity, substrate specificity, and its role in orchestrating complex cellular processes such as DNA synthesis, repair, and chromatin remodeling. The study of Cdk2 Substrates also extends to research on cell differentiation, where Cdk2's role in modulating transitions between different cell cycle phases is of particular interest. In addition, Cdk2 Substrates are used to explore the molecular mechanisms that underlie cell cycle checkpoints, which ensure that cells do not progress to the next phase of the cycle until certain conditions are met. The availability of these substrates has significantly advanced research in fields such as molecular biology, cancer research, and cell biology, providing essential tools for dissecting the regulatory networks that control cell proliferation. View detailed information on our available Cdk2 Substrates by clicking on the product name.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Cdk2 substrate

sc-3056
0.5 mg/0.1 ml
$96.00
(0)

Cdk2 substrate exhibits a unique structural conformation that facilitates its recognition by Cdk2, allowing for specific phosphorylation events. The substrate's interaction with the enzyme is marked by hydrophobic and ionic interactions, enhancing substrate specificity. This dynamic engagement influences the enzyme's catalytic efficiency, promoting rapid turnover rates. Additionally, the substrate's conformational flexibility plays a crucial role in modulating the accessibility of phosphorylation sites, impacting cellular signaling cascades.