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Mouse Anti-CDK2 Recombinant Antibody (CBFYC-1593) (CBMAB-C1652-FY)

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Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBFYC-1593
Antibody Isotype
IgG2a, κ
Application
WB, IP

Basic Information

Immunogen
Human recombinant Cdk2.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
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
The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution.
Entrez Gene ID
Human1017
Mouse12566
Rat362817
UniProt ID
HumanP24941
MouseP97377
RatQ63699
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 2.7.1
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).
More Infomation

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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