This recombinant human Serine-protein kinase ATM is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
The protein serine-protein kinase ATM is a crucial regulator of the cellular response to DNA damage, particularly DNA double-strand breaks (DSBs) [1][2]. ATM phosphorylates multiple factors in the extensive DNA damage response network, thereby regulating cell cycle checkpoints and DNA repair [3]. Additionally, ATM mediates cell-cycle checkpoint activation and DNA double-strand break repair [4]. The kinase domain of ATM is essential for activating p53 transcriptional activity, which is crucial for the cell's response to DNA damage [5].
Furthermore, ATM regulates protein phosphatase 1 in response to DNA damage, phosphorylating its substrates on serines or threonines followed by glutamine [6]. The protein ATM plays a role in the DNA damage response, signaling in response to redox signals, controlling metabolic processes, and maintaining mitochondrial homeostasis [7]. Loss of ATM leads to primary immunodeficiency and greatly increased risk for lymphoid malignancies, highlighting its role as a master regulator of the DNA damage response [8]. ATM also activates p53 and ATR by ionizing radiation, and it associates with and phosphorylates p53, mapping the region of interaction [9] [10] [11]. Additionally, ATM transduces genomic stress signals to halt cell cycle progression and promote DNA repair in response to DNA damage [12].
References:
[1] Y. Shiloh and Y. Ziv, The atm protein: the importance of being active, The Journal of Cell Biology, vol. 198, no. 3, p. 273-275, 2012. https://doi.org/10.1083/jcb.201207063
[2] S. Nyati, G. Young, B. Ross, & A. Rehemtulla, Quantitative and dynamic imaging of atm kinase activity,, p. 131-145, 2017. https://doi.org/10.1007/978-1-4939-6940-1_9
[3] N. Fernandes, Y. Sun, S. Chen, P. Paul, R. Shaw, L. Cantleyet al., Dna damage-induced association of atm with its target proteins requires a protein interaction domain in the n terminus of atm, Journal of Biological Chemistry, vol. 280, no. 15, p. 15158-15164, 2005. https://doi.org/10.1074/jbc.m412065200
[4] C. Bakkenist, R. Czambel, P. Hershberger, H. Tawbi, J. Beumer, & J. Schmitz, A quasi-quantitative dual multiplexed immunoblot method to simultaneously analyze atm and h2ax phosphorylation in human peripheral blood mononuclear cells, Oncoscience, vol. 2, no. 5, p. 542-554, 2015. https://doi.org/10.18632/oncoscience.162
[5] G. Turenne, P. Paul, L. Laflair, & B. Price, Activation of p53 transcriptional activity requires atm's kinase domain and multiple n-terminal serine residues of p53, Oncogene, vol. 20, no. 37, p. 5100-5110, 2001. https://doi.org/10.1038/sj.onc.1204665
[6] X. Tang, Z. Hui, X. Cui, R. Garg, M. Kastan, & B. Xu, A novel atm-dependent pathway regulates protein phosphatase 1 in response to dna damage, Molecular and Cellular Biology, vol. 28, no. 8, p. 2559-2566, 2008. https://doi.org/10.1128/mcb.01711-07
[7] M. Rahim, Y. Cherniavskyi, D. Tieleman, & S. Dames, Nmr– and md simulation–based structural characterization of the membrane-associating fatc domain of ataxia telangiectasia mutated, Journal of Biological Chemistry, vol. 294, no. 17, p. 7098-7112, 2019. https://doi.org/10.1074/jbc.ra119.007653
[8] M. Milanovic, Z. Shao, V. Estes, X. Wang, D. Menolfi, X. Linet al., Fatc domain deletion compromises atm protein stability, blocks lymphocyte development, and promotes lymphomagenesis, The Journal of Immunology, vol. 206, no. 6, p. 1228-1239, 2021. https://doi.org/10.4049/jimmunol.2000967
[9] J. Myers and D. Chen, Rapid activation of atr by ionizing radiation requires atm and mre11, Journal of Biological Chemistry, vol. 281, no. 14, p. 9346-9350, 2006. https://doi.org/10.1074/jbc.m513265200
[10] C. Canman, D. Lim, K. Cimprich, Y. Taya, K. Tamai, K. Sakaguchiet al., Activation of the atm kinase by ionizing radiation and phosphorylation of p53, Science, vol. 281, no. 5383, p. 1677-1679, 1998. https://doi.org/10.1126/science.281.5383.1677
[11] K. Khanna, K. Keating, S. Kozlov, S. Scott, M. Gatei, K. Hobsonet al., Atm associates with and phosphorylates p53: mapping the region of interaction, Nature Genetics, vol. 20, no. 4, p. 398-400, 1998. https://doi.org/10.1038/3882
[12] N. Kanu and A. Behrens, Atmin defines an nbs1-independent pathway of atm signalling, The Embo Journal, vol. 26, no. 12, p. 2933-2941, 2007. https://doi.org/10.1038/sj.emboj.7601733
