Date published: 2025-11-21

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Cdk2 Inhibitors

Cyclin-dependent kinase 2 (Cdk2) inhibitors represent a class of chemical compounds that play a pivotal role in regulating the progression of the cell cycle. Cdk2, a member of the cyclin-dependent kinase family, is a serine/threonine kinase enzyme that partners with various cyclins to control the transition between different phases of the cell cycle. The inhibitors targeting Cdk2 are designed to modulate its activity, primarily by preventing the interaction between Cdk2 and its binding partner, cyclin. By doing so, these inhibitors disrupt the phosphorylation events that are critical for cell cycle progression. Cdk2 inhibitors exhibit a diverse range of chemical structures, each tailored to specifically interact with the active site of the enzyme. These compounds often contain conserved motifs that are crucial for binding to the ATP-binding pocket of Cdk2. By binding to this pocket, the inhibitors compete with ATP molecules, thereby obstructing the enzymatic activity of Cdk2. This binding interaction leads to a halt in the phosphorylation of key substrates involved in cell cycle progression, ultimately resulting in cell cycle arrest. The rational design of Cdk2 inhibitors involves a detailed understanding of the enzyme's structural features and catalytic mechanisms, allowing chemists to fine-tune the compounds for optimal binding affinity and specificity.

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Items 41 to 50 of 53 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Cdk/Crk Inhibitor

784211-09-2sc-203872
1 mg
$290.00
(0)

Cdk/Crk Inhibitor acts as a potent modulator of Cdk2, characterized by its ability to form stable complexes through unique hydrogen bonding and hydrophobic interactions. This compound induces a significant alteration in the enzyme's tertiary structure, which disrupts substrate recognition. Its reaction kinetics suggest a non-competitive inhibition pattern, influencing the phosphorylation cascade. Furthermore, the inhibitor's distinct molecular architecture enhances selectivity towards specific protein interactions, thereby fine-tuning cellular signaling dynamics.

AT7519

844442-38-2sc-364416
sc-364416A
sc-364416B
sc-364416C
5 mg
10 mg
100 mg
1 g
$207.00
$246.00
$1025.00
$3065.00
1
(0)

AT7519 is a potent CDK inhibitor that targets CDK2 and other kinases, inducing cell cycle arrest and apoptosis by preventing substrate phosphorylation.

CR8, (S)-Isomer

1084893-56-0sc-311307
5 mg
$201.00
(0)

CR8, (S)-Isomer, exhibits remarkable specificity in its interaction with Cdk2, primarily through its unique steric configuration that facilitates precise binding. This compound alters the enzyme's active site conformation, leading to a notable decrease in catalytic efficiency. Its kinetic profile reveals a mixed inhibition mechanism, impacting both substrate affinity and turnover rate. Additionally, CR8's unique electronic properties contribute to its selective engagement with key regulatory motifs, modulating cellular pathways with high precision.

Dinaciclib

779353-01-4sc-364483
sc-364483A
5 mg
25 mg
$242.00
$871.00
1
(0)

Dinaciclib is a CDK2/9 inhibitor that disrupts cell cycle progression and transcription by inhibiting phosphorylation of CDK2 substrates and RNA polymerase II.

TAK 165

366017-09-6sc-361372
sc-361372A
10 mg
50 mg
$139.00
$781.00
(0)

TAK 165 demonstrates a distinctive binding affinity for Cdk2, characterized by its ability to stabilize an inactive conformation of the enzyme. This compound engages in specific hydrogen bonding and hydrophobic interactions, effectively disrupting the enzyme's catalytic cycle. Its reaction kinetics indicate a competitive inhibition pattern, influencing substrate binding dynamics. Furthermore, TAK 165's unique structural features allow it to selectively modulate downstream signaling pathways, showcasing its intricate role in cellular regulation.

Cdk2/9 Inhibitor Inhibitor

507487-89-0sc-221411
5 mg
$416.00
1
(0)

Cdk2/9 Inhibitor exhibits a remarkable selectivity for Cdk2, engaging in unique electrostatic interactions that alter the enzyme's active site conformation. This compound effectively impedes the phosphorylation process by stabilizing a non-productive enzyme-substrate complex. Its kinetic profile reveals a non-competitive inhibition mechanism, impacting the overall enzymatic turnover rate. Additionally, the inhibitor's structural motifs facilitate specific interactions with regulatory proteins, influencing cellular cycle progression.

Cdk1/2 Inhibitor III

443798-55-8sc-202530
1 mg
$198.00
3
(1)

Cdk1/2 Inhibitor III demonstrates a distinctive binding affinity for Cdk2, characterized by its ability to form hydrogen bonds that enhance the stability of the enzyme-inhibitor complex. This compound disrupts the normal catalytic cycle by inducing conformational changes that hinder substrate access. Its unique reaction kinetics suggest a mixed inhibition model, affecting both substrate binding and catalytic efficiency. Furthermore, the inhibitor's structural features allow for selective modulation of protein-protein interactions, impacting downstream signaling pathways.

BML-259

267654-00-2sc-202505
5 mg
$127.00
1
(0)

BML-259 exhibits a remarkable selectivity for Cdk2, engaging in specific hydrophobic interactions that stabilize its binding. This compound alters the enzyme's active site geometry, effectively blocking substrate recognition and impeding phosphorylation processes. Its kinetic profile reveals a non-competitive inhibition mechanism, influencing the overall enzymatic turnover. Additionally, BML-259's unique structural motifs facilitate targeted disruption of regulatory networks, underscoring its role in cellular signaling modulation.

R547

741713-40-6sc-364596
sc-364596A
2 mg
5 mg
$375.00
$395.00
(0)

R547 is a selective CDK2 inhibitor that binds to the ATP-binding site, inhibiting substrate phosphorylation and leading to cell cycle arrest.

PHA 767491 hydrochloride

942425-68-5sc-204187
sc-204187A
10 mg
50 mg
$194.00
$786.00
3
(2)

PHA 767491 hydrochloride demonstrates a distinctive affinity for Cdk2, characterized by its ability to form hydrogen bonds with key amino acid residues within the enzyme's active site. This interaction leads to a conformational change that hinders substrate access, effectively reducing catalytic efficiency. The compound's unique electronic properties enhance its binding stability, while its specific steric configuration allows for selective interference in cell cycle regulation pathways, highlighting its intricate role in cellular dynamics.