This DEK protein 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 DEK is a nuclear phosphoprotein with two functional domains, SaP and DNA binding/multimerization, several phosphorylation sites, and three highly acidic domains [1]. It is ubiquitously expressed in multicellular organisms and some unicellular organisms [2]. DEK is involved in altering the structure of DNA by introducing positive supercoils, which may affect the efficiency of DNA replication and the activity of chromatin [3][4][5].
DEK is implicated in gene regulation, as it binds to DNA in a structure-specific manner, affecting chromatin accessibility to the replication machinery [6][5]. DEK's overexpression has been associated with poor prognosis in various cancers, such as lung cancer, ovarian tumors, cervical cancer, hepatocellular carcinoma, and breast cancer [2][7][8][9][10]. DEK positively regulates cell proliferation, invasion, and angiogenesis in lung cancer [2]. DEK is involved in inhibiting differentiation and facilitating cellular transformation [8]. In cervical cancer, DEK overexpression is induced by high-risk HPV E7 protein and is dependent on retinoblastoma protein (Rb) function, suggesting its crucial role in cervical cancer progression [7]. DEK's association with structured DNA templates and its ability to induce positive supercoils into circular DNA templates have led to the notion that DEK serves as an architectural protein [6][1]. Furthermore, DEK has been identified as a poly(ADP-ribose) acceptor in apoptosis and mediates resistance to genotoxic stress [4].
References:
[1] T. Waldmann, C. Eckerich, M. Baack, & C. Gruss, The ubiquitous chromatin protein dek alters the structure of dna by introducing positive supercoils, Journal of Biological Chemistry, vol. 277, no. 28, p. 24988-24994, 2002. https://doi.org/10.1074/jbc.m204045200
[2] Q. Zhou, X. Deng, J. Yang, H. Jiang, M. Qiao, H. Liuet al., Oncogene dek is highly expressed in lung cancerous tissues and positively regulates cell proliferation as well as invasion, Oncology Letters, 2018. https://doi.org/10.3892/ol.2018.8436
[3] V. Alexiadis, T. Waldmann, J. Andersen, M. Mann, R. Knippers, & C. Gruss, The protein encoded by the proto-oncogene dek changes the topology of chromatin and reduces the efficiency of dna replication in a chromatin-specific manner, Genes & Development, vol. 14, no. 11, p. 1308-1312, 2000. https://doi.org/10.1101/gad.14.11.1308
[4] F. Kappes, J. Fahrer, M. Khodadoust, A. Tabbert, C. Straßer, N. Mor-Vakninet al., Dek is a poly(adp-ribose) acceptor in apoptosis and mediates resistance to genotoxic stress, Molecular and Cellular Biology, vol. 28, no. 10, p. 3245-3257, 2008. https://doi.org/10.1128/mcb.01921-07
[5] M. Sammons, S. Wan, N. Vogel, E. Mientjes, G. Grosveld, & B. Ashburner, Negative regulation of the rela/p65 transactivation function by the product of the dek proto-oncogene, Journal of Biological Chemistry, vol. 281, no. 37, p. 26802-26812, 2006. https://doi.org/10.1074/jbc.m600915200
[6] S. Han, Y. Xuan, S. Liu, M. Zhang, D. Jin, R. Jinet al., Clinicopathological significance of dek overexpression in serous ovarian tumors, Pathology International, vol. 59, no. 7, p. 443-447, 2009. https://doi.org/10.1111/j.1440-1827.2009.02392.x
[7] Q. Wu, Z. Li, H. Lin, L. Han, S. Liu, & Z. Lin, Dek overexpression in uterine cervical cancers, Pathology International, vol. 58, no. 6, p. 378-382, 2008. https://doi.org/10.1111/j.1440-1827.2008.02239.x
[8] H. Yi, Y. Liu, Y. Peng, J. Pan, J. Zhou, Z. Liuet al., Overexpression of dek gene is correlated with poor prognosis in hepatocellular carcinoma, Molecular Medicine Reports, vol. 11, no. 2, p. 1318-1323, 2014. https://doi.org/10.3892/mmr.2014.2781
[9] Y. Guo and Y. Wu, Dek: a novel early screening and prognostic marker for breast cancer, Molecular Medicine Reports, vol. 12, no. 5, p. 7491-7495, 2015. https://doi.org/10.3892/mmr.2015.4380
[10] T. Wise‐Draper, R. Morreale, T. Morris, R. Mintz-Cole, E. Hoskins, S. Balsitiset al., Dek proto-oncogene expression interferes with the normal epithelial differentiation program, American Journal of Pathology, vol. 174, no. 1, p. 71-81, 2009. https://doi.org/10.2353/ajpath.2009.080330
