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Validated All-in-One™ qPCR Primer for CDK2(NM_001798.4) Search again
Product ID:
HQP090157
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CDKN2, p33(CDK2)
Gene Description:
cyclin dependent kinase 2
Target Gene Accession:
NM_001798.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2. It is a catalytic subunit of the cyclin-dependent protein kinase complex, whose activity is restricted to the G1-S phase, and essential for cell cycle G1/S phase transition. This protein associates with and regulated by the regulatory subunits of the complex including cyclin A or E, CDK inhibitor p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B). Its activity is also regulated by its protein phosphorylation. Two alternatively spliced variants and multiple transcription initiation sites of this gene have been reported.
Gene References into function
- Cyclin A/Cdk2 and cyclin E/cdk2 continuously shuttle between the nucleus and the cytoplasm
- results argue that TTK-associated CDK2 may function to maintain target-specific phosphorylation of RNA Pol II that is essential for Tat transactivation of HIV-1 promoter
- Activation mechanism role of cyclin binding versus phosphorylation
- CDK2/cyclin E is required for Tat-dependent transcription in vitro.
- CDK2 binding to cyclin E is required to drive cells from G(1) into S phase
- Interferon gamma reduces the activity of Cdk4 and Cdk2, inhibiting he G1 cell cycle in human hepatocellular carcinoma cells.
- CDK2 is not required for sustained cell division.
- Data suggest that the interaction between PKCeta and cyclin E is carefully regulated, and is correlated with the inactivated form of the cyclin E/Cdk2 complex.
- IRF1 represses CDK2 gene expression by interfering with SP1-dependent transcriptional activation.
- role in regulating Cdc25A half life
- TGF-beta 1 inhibition requires early G(1) induction and stabilization of p21 protein, which binds to & inhibits cyclin E-CDK2 and cyclin A-CDK2 kinase activity rather than direct modulation of cyclin or CDK protein levels as seen in other systems.
- Cdk2 has a role in phosphorylation of the NF-Y transcription factor
- CDK2 has a role in the G2 DNA damage checkpoint
- Kaposi's sarcoma-associated herpesvirus K-bZIP physically associates with cyclin-CDK2 and downmodulates its kinase activity.
- it is evident that B-Myb protein may promote cell proliferation by a non-transcriptional mechanism that involves release of active cyclin/cyclin dependent kinase 2 from cyclin-dependent inhibitor 1C p57(KIP2)
- Inhibition of Cdk2 by 1,25-(OH)2D3 may thus involve two mechanisms: 1) reduced nuclear Cdk2 available for cyclin binding and activation and 2) impairment of cyclin E-Cdk2-dependent p27 degradation through cytoplasmic mislocalization of Cdk2.
- kinetic insight into the basis for selecting suboptimal specificity determinants for the phosphorylation of cellular substrates
- multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation
- CDK2 binds to SU9516 at Leu83 and Glu81
- CDK2 activation process through phosphorylation is examined using 2D PAGE
- Epstein-Barr virus can inhibit genotoxin-induced G1 arrest downstream of p53 by preventing the inactivation of CDK2
- p220 is an essential downstream component of the cyclin E/Cdk2 signaling pathway and functions to coordinate multiple elements of the G1/S transition.
- CDK2-cyclin E, without prior CDK4-cyclin D activity, can phosphorylate and inactivate pRb, activate E2F, and induce DNA synthesis.
- significant difference in their biochemical properties between CDK4/cyclin D1 and CDK2/cyclin A affecting regulation of cellular RB function
- cyclin-dependent kinase (CDK)2, -4, and -6 were down-regulated from the myelocytes/metamyelocytes stages and onward
- CDK2 complexes have roles in G(1)/S deregulation and tumor progression
- CDK2 regulates beta-catenin phosphorylation/ degradation
- Cdk2 and Cdk4 phosphorylate human Cdt1 and induce its degradation
- Binding to Cdk2-cyclin A is accompanied by p27 folding, and kinetic data suggest a sequential mechanism that is initiated by binding to cyclin A
- We also found that cyclin A/CDK2 phosphorylates Axin, thereby enhancing its association with beta-catenin.
- study provides evidence that the cyclin A1-cyclin dependent kinase 2 complex plays a role in several signaling pathways important for cell cycle control and meiosis
- interacts with dephosphorylated NIRF
- cyclin A-cdk2 plays an ancillary noncatalytic role in the ubiquitination of p27(KIP1) by the SCF(skp2) complex
- Results identify an important role for CDK2 in the maintenance of genomic stability, acting via an ATM- and ATR-dependent pathway.
- after CDK4/6 inactivation, the fate of pancreatic tumor cells depends on the ability to modulate CDK2 activity
- Data suggest that cyclin D1-Cdk2 complexes mediate some of the transforming effects of cyclin D1 and demonstrate that the cyclin D1-Cdk2 fusion protein is a useful model to investigate the biological functions of cyclin D1-Cdk2 complexes.
- These findings establish a novel function for cyclin A1 and CDK2 in DNA double strand break repair following radiation damage.
- Phosphborylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of CDK2.
- cyclin A/Cdk2 has a role as a progesterone receptor coactivator
- CDK2 depletion suppressed growth and cell cycle progression in melanoma and may be a suitable drug target in melanoma.
- Inhibition of CDK2 kinase by indole-3-carbinol is accompanied by selective alterations in cyclin E composition.
- molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRK
- Results demonstrate that a peptide derived from the alpha5 helix of cyclin A significantly inhibits kinase activity of complexes harboring CDK2, and forms stable complexes with CDK2-cyclin A.
- crystal structure of phospho-CDK2 in complex with a truncated cyclin E1 (residues 81-363) at 2.25 A resolution
- CDK2-BRCA1-Nucleophosmin pathway coordinately functions in cell growth and tumor progression pathways.
- HTm4 binding to KAP.Cdk2.cyclin A complex enhances the phosphatase activity of KAP, dissociates cyclin A, and facilitates KAP dephosphorylation of Cdk2
- Results present a comprehensive description of the dynamic behavior of cyclin-dependent kinase 2 in complex with cyclin A.
- Puralpha has been shown to colocalize with cyclin A/Cdk2 and to coimmunoprecipitate with cyclin A during S-phase and we show that this interaction is mediated by a specific affinity of Puralpha for Cdk2.
- Rapid binding of p27 domain 1 to cyclin A tethers the inhibitor to the binary Cdk2/cyclin A complex
- CDK2 translational down-regulation may be a key regulatory event in replicative senescence of endothelial cells.
- origin recognition complex 2 has an unexpected role in CDK2 activation, a linkage that could be important for maintaining genomic stability
- Cdk2 destabilizes p21 via the cy2 cyclin-binding motif and p21 phosphorylation
- Our results demonstrate that differential regulation of Cdc2 and Cdk2 activity by different doses of doxorubicin may contribute to the induction of two modes of cell death in hepatoma cells, either apoptosis or cell death through mitotic catastrophe.
- CINP is part of the Cdc7-dependent mechanism of origin firing and a functional and physical link between Cdk2 and Cdc7 complexes at the origins
- CDK2 inhibition modifies the dynamics of chromatin-bound minichromosome maintenance complex and replication protein A
- results indicate that CDK2 participates in Tat-mediated HIV-1 transcription and may serve as a potential therapeutic target
- Cdk2 inhibition decreases the efficiency of chemical induction of KSHV lytic transcripts ORF 50 and 26. Importantly, Cdk2 activity is also essential for replication in other human herpesviruses
- A new concept indicates in this review that both Cdk2 and/or Cdc2 can drive cells through G1/S phase in parallel.
- Cdk2 dependent phosphorylation(s) cannot be a critical trigger of replicon initiation in response to reoxygenation after several hours of hypoxia, at least in the T24 cells studied
- We propose that during TNFalpha-induced apoptosis, PKCdelta-mediated phosphorylation of p21(WAF1/CIP1) at (146)Ser attenuates the Cdk2 binding of p21(WAF1/CIP1) and thereby upregulates Cdk2 activity.
- molecular analysis of the CDK5/p25 and CDK2/cyclin A systems
- Cyclin-dependent kinases regulate the transcriptional activity of FOXM1c; a combination of three phosphorylation sites mediates the Cyclin E and Cyclin A/CDK2 effects.
- Here, we show that human papillomavirus type 16 16E1--E4 is also able to associate with cyclin A and Cdk2 during the G2 phase of the cell cycle.
- The interaction between roscovitine and cyclin-dependent kinase 2 (cdk2) was investigated by performing correlated ab initio quantum-chemical calculations.
- the phospho-CDK2/cyclin A recruitment site has a role in substrate recognition
- Phosphorylation of the linker histone H1 by CDK regulates its binding to HP1alpha
- suggest a novel retinoic acid (RA)-signaling, by which RA-induced p21 induction and complex formation with cyclin E/CDK2 diverts CDK2 function from normally driving proliferation to alternatively promoting apoptosis
- Membrane depolarization may stimulate cellular proliferation by augmenting the expression of cyclin E leading to increases in Cdk2 activity and RB phosphorylation in a neuroblastoma cell line.
- the Chk1-mediated S-phase checkpoint targets initiation factor Cdc45 via a Cdc25A/Cdk2-independent mechanism
- Breast cancer cells lacking cancer predisposition genes BRCA1 are more sensitive to CDK2 inhibitors.
- analysis of the NBI1-binding site on cyclin A which inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A
- progression of melanoma is associated with changes in CDK-2 expression level
- functional interaction between CDK2 and FOXO1 provides a mechanism that regulates apoptotic cell death after DNA strand breakage
- Kinetic and crystallographic analyses of CDK2-cyclin A complexes reveal that this inhibitory mechanism operates through steric blockade of peptide substrate binding.
- Review highlights an alternative role for CDK2 in the regulation of progesterone receptor signaling.
- TopBP1 necessary for the G(1)/S transition: one for activating cyclin E/CDK2 kinase and the other for loading replication components onto chromatin to initiate DNA synthesis.
- Our results demonstrate that CDK2 is capable of autophosphorylation at Thr160.
- results argue that Mdm2 is needed for full inhibition of Cdk2 activity by p21, thereby positively contributing to p53-dependent cell cycle arrest
- Both Cdk1 and -2 require cyclin binding and T loop phosphorylation for full activity.
- The structure of phospho-CDK2/cyclin B is reported. pCDK2/cyclin B is less discriminatory in substrate recognition than CDK2/cyclin A & has properties of both an S-phase & an M-phase kinase. CDK2/cyclin B is effective against S phase substrates.
- ATRIP is a CDK2 substrate, and CDK2-dependent phosphorylation of S224 regulates the ability of ATR-ATRIP to promote cell cycle arrest in response to DNA damage
- Phosphorylation on a conserved Thr14 can inhibit activities of both the kinases, but phosphorylating another conserved Tyr15, however, can lead to totally opposite inhibition and stimulation consequences in CDK2 and CDK5.
- The conserved rigid regions are important for nucleotide binding, catalysis, and substrate recognition; most flexible regions correlate with those where large conformational changes occur during CDK2 regulation processes.
- cdk2 activity is necessary for the survival of human DLBCL.
- major Cdk2-dependent multiple gene regulatory events are present in pemphigus vulgar
- serum starvation induces G1 arrest through suppression of Skp2-dependent CDK2 activity and Skp2-independent CDK4 activity in human SK-OV-3 ovarian cancer cells
- Findings strongly demonstrate that retinoblastoma (RB) and cyclin-dependent kinase 2 (CDK2) on one side and cytokeratin 8 (CK8) and epidermal growth factor receptor 2 (HER2) on the other may affect the clinical course of the disease in 56% of patients.
- Cyclin E and SV40 small T antigen cooperate to bypass quiescence and contribute to transformation by activating CDK2 in human fibroblasts
- Bim-mediated apoptosis following actin damage due to deregulation of Cdk2 and the cell cycle by the absence of functional p53.
- G2 phase cyclin A/cdk2 controls the timing of entry into mitosis by controlling the subsequent activation of cyclin B/cdk1, but also has an unexpected role in coordinating the activation of cyclin B/cdk1 at the centrosome and in the nucleus
- disruption of the spindle-assembly checkpoint does not directly influence p53 activation, but the shortening of the mitotic arrest allows cyclin E-CDK2 to be activated before the accumulation of p21(CIP1/WAF1).
- Results suggest that GSK-3 regulates nuclear p27 Kip1 expression through downregulation of Skp2 expression and regulates p27 Kip1 assembly with CDK2, playing a critical role in the G0/G1 arrest associated with intestinal cell differentiation.
- The structures of fully active cyclin-dependent kinase-2 (CDK2)complexed with ATP and peptide substrate, CDK2 after the catalytic reaction, and CDK2 inhibited by phosphorylation at Thr14/Tyr15 were studied using molecular dynamics simulations.
- Cdk2-associated complexes, by targeting SHP-1 for proteolysis, counteract the ability of SHP-1 to block cell cycle progression of intestinal epithelial cells
- Cyclin A-CDK activity during G(1) would result in an inhibition of progression into the S phase.
- the cyclin A-CDK2 complex may be a potential effector of NFATs, specifically NFATc1, in mediating SMC multiplication leading to neointima formation.
- Cdk2 negatively regulates the activity of hPXR, and suggest an important role for Cdk2 in regulating hPXR activity and CYP3A4 expression in hepatocytes passing through the cell cycle
- This suggests an important role for CDK2 in cell cycle regulation in hESCs that are likely to bear significant impacts on the maintenance of their pluripotent phenotype.
- Cyclin A assembles with Cdk1 only after complex formation with Cdk2 reaches a plateau during late S and G2 phases.
- These findings establish phosphorylation events by CDKs 1 and 2 as key regulators of Discs Large 1 localisation and function.
- These results demonstrate that double phosphorylation of CDK2 peptides increases the stoichiometry of metal ion binding, and hence may contribute to the previously observed regulation of CDK2 activity by metal ions.
- the pathway of apoptin-induced apoptosis and show that it essentially depends on abnormal phosphatidylinositol 3-kinase (PI3-kinase)/Akt activation, resulting in the activation of the cyclin-dependent kinase CDK2
- disruption of Smad2 function by CDK2 phosphorylation acts as a mechanism for TGF-beta resistance in multiple myeloma.