CDK4/CycD2 Kinase TR-FRET Detection Kit
Item | Cat# | Price |
TR-FRET Detection Kit | SNB-B-0013 | Inquiry |
Compound Test Services | CT-001 | $1,050 per 384w plate (Up To 16 cpds Dose) |
Product Description
Cyclin-dependent kinases (CDKs) are a family of serine/threonine kinases that play central roles in regulating the eukaryotic cell cycle. Their activity depends on association with specific cyclins, which control CDK activation at distinct cell cycle phases. For example, CDK4/6–cyclin D complexes drive G1 phase progression, while CDK1–cyclin B controls entry into mitosis. CDKs function by phosphorylating key substrates that govern DNA replication, mitotic entry, and transcriptional regulation. Beyond cell cycle control, several CDKs (e.g., CDK7, CDK9) are involved in transcriptional regulation via phosphorylation of RNA polymerase II. Dysregulation of CDK activity is frequently observed in cancer, leading to uncontrolled proliferation. Consequently, selective CDK inhibitors such as palbociclib, ribociclib, and abemaciclib have been developed as targeted therapies, particularly for breast cancer, underscoring the critical role of CDKs in both normal cellular homeostasis and oncogenesis.
Screeningbio’s TR-FRET CDKs kinase assay kit is designed to measure the relative activity levels of kinases. The kit uses a specific CDKs kinase substrate and detection reagents to evaluate kinase activity. Cyclin-dependent kinases (CDKs) constitute a large family, including CDK1/3/4/6/7/9/10/12/13/15–18, which specifically recognize and phosphorylate the Retinoblastoma-associated protein (Rb) at serine residue 780 (S780). Therefore, this kit employs an optimized Rb (S780) peptide as a substrate, coupled with TR-FRET LA(TR-FRET Acceptor) and TR-FRET Solar Eu conjugates(TR-FRET Donor), together with a phospho-Rb (S780)–specific antibody. This allows kinase activity to be quantified by detecting the level of phosphorylated substrate.
Data
Target Background
Cyclin-dependent kinase 4 (CDK4) is a serine/threonine kinase that plays a critical role in controlling the G1 to S phase transition of the eukaryotic cell cycle. CDK4 forms an active complex with D-type cyclins (Cyclin D1, D2, or D3) in response to mitogenic signals such as growth factors. This CDK4/Cyclin D complex phosphorylates the retinoblastoma protein (Rb), leading to the release of E2F transcription factors that activate genes essential for DNA replication and cell-cycle progression.
CDK4 activation requires dual regulation through cyclin binding and phosphorylation by CDK-activating kinase (CAK). Its activity is negatively regulated by cyclin-dependent kinase inhibitors (CKIs), particularly p16^INK4a and p21^Cip1, which maintain proper cell-cycle checkpoints and prevent uncontrolled proliferation.
Physiologically, CDK4 integrates extracellular mitogenic cues with intracellular growth control, making it essential for normal development and tissue homeostasis. However, dysregulation of CDK4—through cyclin D overexpression, p16 inactivation, or CDK4 gene amplification—is frequently observed in cancers such as melanoma, breast cancer, and glioblastoma.
Given its oncogenic potential, CDK4 has become an important therapeutic target. Selective CDK4/6 inhibitors, such as palbociclib, ribociclib, and abemaciclib, are now widely used in cancer therapy to induce G1 cell-cycle arrest and inhibit tumor growth.