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Mouse Anti-CDK2 Recombinant Antibody (CBXC-0315) (CBMAB-C3213-CQ)

This product is a mouse antibody that recognizes CDK2. The antibody CBXC-0315 can be used for immunoassay techniques such as: ELISA, IF, IHC, WB.
See all CDK2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXC-0315
Antibody Isotype
IgG2b
Application
ELISA, IF, IHC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Cyclin Dependent Kinase 2
Introduction
This gene encodes a member of a family of serine/threonine protein kinases that participate in cell cycle regulation. The encoded protein is the catalytic subunit of the cyclin-dependent protein kinase complex, which regulates progression through the cell cycle. Activity of this protein is especially critical during the G1 to S phase transition. This protein associates with and regulated by other subunits of the complex including cyclin A or E, CDK inhibitor p21Cip1 (CDKN1A), and p27Kip1 (CDKN1B). Alternative splicing results in multiple transcript variants.
Entrez Gene ID
UniProt ID
Alternative Names
Cyclin Dependent Kinase 2; Cell Division Protein Kinase 2; P33 Protein Kinase; EC 2.7.11.22; CDKN2; CDC2-Related Protein Kinase; Cyclin-Dependent Kinase 2; P33(CDK2); EC 2.7.11;
Function
Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity).
Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity).
Phosphorylates CDK2AP2 (PubMed:12944431).
Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878).
Biological Process
Anaphase-promoting complex-dependent catabolic process Source: Reactome
Cell division Source: UniProtKB-KW
Cellular response to nitric oxide Source: UniProtKB
Centriole replication Source: UniProtKB
Centrosome duplication Source: UniProtKB
DNA repair Source: UniProtKB-KW
DNA replication Source: UniProtKB
DNA replication initiation Source: Reactome
G1/S transition of mitotic cell cycle Source: GO_Central
G2/M transition of mitotic cell cycle Source: Reactome
Granulocyte differentiation Source: Reactome
Histone phosphorylation Source: CAFA
Meiotic cell cycle Source: UniProtKB
Mitotic G1 DNA damage checkpoint Source: UniProtKB
Peptidyl-serine phosphorylation Source: UniProtKB
Positive regulation of cell population proliferation Source: UniProtKB
Protein phosphorylation Source: UniProtKB
Ras protein signal transduction Source: BHF-UCL
Regulation of G2/M transition of mitotic cell cycle Source: GO_Central
Regulation of gene expression Source: GO_Central
Regulation of gene silencing Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Signal transduction Source: GO_Central
Telomere maintenance via telomerase Source: Reactome
Cellular Location
Centrosome; Cajal body; Cytoplasm; Endosome. Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)2D3.
PTM
Phosphorylated at Thr-160 by CDK7 in a CAK complex (PubMed:28666995). Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A.
Nitrosylated after treatment with nitric oxide (DETA-NO).

Bitencourt-Ferreira, G., Duarte da Silva, A., & Filgueira, D. A. J. (2021). Application of Machine Learning Techniques to Predict Binding Affinity for Drug Targets: A Study of Cyclin-dependent Kinase 2. Current medicinal chemistry, 28(2), 253-265.

Zhang, J. Q. J., Burgess, J., Stepanova, D., Saravanabavan, S., Wong, A. T., Kaldis, P., & Rangan, G. K. (2020). Role of cyclin-dependent kinase 2 in the progression of mouse juvenile cystic kidney disease. Laboratory Investigation, 100(5), 696-711.

Yun, F., Cheng, C., Ullah, S., & Yuan, Q. (2020). Design, synthesis and biological evaluation of novel histone deacetylase1/2 (HDAC1/2) and cyclin-dependent Kinase2 (CDK2) dual inhibitors against malignant cancer. European journal of medicinal chemistry, 198, 112322.

Faber, E. B., Wang, N., & Georg, G. I. (2020). Review of rationale and progress toward targeting cyclin-dependent kinase 2 (CDK2) for male contraception. Biology of reproduction, 103(2), 357-367.

Volkart, P. A., Bitencourt-Ferreira, G., Souto, A. A., & de Azevedo, W. F. (2019). Cyclin-dependent kinase 2 in cellular senescence and cancer. A structural and functional review. Current drug targets, 20(7), 716-726.

Mohammad, T., Batra, S., Dahiya, R., Baig, M. H., Rather, I. A., Dong, J. J., & Hassan, I. (2019). Identification of high-affinity inhibitors of cyclin-dependent kinase 2 towards anticancer therapy. Molecules, 24(24), 4589.

Tadesse, S., Caldon, E. C., Tilley, W., & Wang, S. (2018). Cyclin-dependent kinase 2 inhibitors in cancer therapy: an update. Journal of medicinal chemistry, 62(9), 4233-4251.

Cherukupalli, S., Chandrasekaran, B., Aleti, R. R., Sayyad, N., Hampannavar, G. A., Merugu, S. R., ... & Karpoormath, R. (2019). Synthesis of 4, 6-disubstituted pyrazolo [3, 4-d] pyrimidine analogues: cyclin-dependent kinase 2 (CDK2) inhibition, molecular docking and anticancer evaluation. Journal of Molecular Structure, 1176, 538-551.

Xia, P., Liu, Y., Chen, J., Coates, S., Liu, D. X., & Cheng, Z. (2018). Inhibition of cyclin-dependent kinase 2 protects against doxorubicin-induced cardiomyocyte apoptosis and cardiomyopathy. Journal of Biological Chemistry, 293(51), 19672-19685.

Cheng, C. W., Leong, K. W., Ng, Y. M., Kwong, Y. L., & Tse, E. (2017). The peptidyl-prolyl isomerase PIN1 relieves cyclin-dependent kinase 2 (CDK2) inhibition by the CDK inhibitor p27. Journal of Biological Chemistry, 292(52), 21431-21441.

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For research use only. Not intended for any clinical use.

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