Date published: 2025-9-13

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Cdc2B Activators

Cdc2B Activators be a class of chemical compounds designed to selectively enhance the activity of the Cdc2B protein, which is a variant of the cell division cycle protein 2 (Cdc2), also known as cyclin-dependent kinase 1 (CDK1). Cdc2 is a pivotal enzyme in eukaryotic cells that plays a crucial role in controlling the progression of the cell cycle, particularly the transition from the G2 phase to mitosis. The 'B' variant suggests a specific form or isoform within the Cdc2 family that may have unique regulatory features or expression patterns. Activators of Cdc2B would be expected to increase its kinase activity, which in turn, would promote the phosphorylation of target substrates involved in cell cycle progression. This could be achieved by enhancing the protein's intrinsic kinase activity, facilitating its association with regulatory subunits like cyclins, or stabilizing the active conformation of the protein. Such compounds might bind directly to Cdc2B or to its regulators and modulate its activity either allosterically or by affecting post-translational modifications that control its function.

Investigating the actions of Cdc2B activators would encompass a range of molecular and cellular techniques. Kinase assays could be employed to directly measure the phosphorylation activity of Cdc2B in the presence of these activators, providing insight into their potency and mode of action. Structural studies, such as X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy, could reveal how these activators interact with Cdc2B at the molecular level, potentially identifying the binding sites and conformational changes associated with activation. Additionally, cell-based assays would be crucial in determining the effect of these activators on cell cycle progression. For instance, flow cytometry could be used to analyze cell cycle distribution after exposure to activators, while live-cell imaging could offer real-time insights into the dynamics of cell division. Such studies would contribute to a comprehensive understanding of the regulatory mechanisms governing Cdc2B activity and how it can be modulated by small molecules.

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