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Protein E7 is a crucial oncoprotein found in high-risk human papillomavirus (HPV) types, such as HPV-16. E7 is a small phosphoprotein that interacts with various cellular proteins to promote cellular transformation. It shares sequence homology with adenovirus E1a protein and simian virus 40 large T antigen [1]. E7 exerts its functions by primarily interacting with the retinoblastoma protein (pRB) and other cellular targets, leading to the inactivation of Rb-related proteins p107 and p130 [2][3]. This inactivation of Rb family proteins by E7 disrupts the normal cell cycle regulation, allowing for uncontrolled cell proliferation [4].
E7 is considered the major transforming protein among HPV oncoproteins and is structurally and functionally similar to adenovirus E1A and SV40 Large T antigen [5]. It binds and destabilizes pRB, p107, and p130, inhibiting their tumor-suppressive functions and promoting cell cycle progression [6]. E7 contains conserved regions, including CR1 at the N-terminal end, CR2 with the LxCxE motif, and CR3 at the C-terminal end, which are crucial for its interactions with molecular targets [7][8].
Moreover, E7 binds to specific domains in the Rb protein, namely RbAB and RbC domains, further interfering with Rb's tumor-suppressive activities [9]. The interaction of E7 with pRB is essential for overcoming cell cycle arrest and promoting cell proliferation [6]. Additionally, E7 can induce abnormal centrosome duplication independently of Rb inactivation, further contributing to its oncogenic potential [4].
References:
[1] N. Gammoh, H. Grm, P. Massimi, & L. Banks, "Regulation of human papillomavirus type 16 e7 activity through direct protein interaction with the e2 transcriptional activator", Journal of Virology, vol. 80, no. 4, p. 1787-1797, 2006. https://doi.org/10.1128/jvi.80.4.1787-1797.2006
[2] A. Helt and D. Galloway, "Destabilization of the retinoblastoma tumor suppressor by human papillomavirus type 16 e7 is not sufficient to overcome cell cycle arrest in human keratinocytes", Journal of Virology, vol. 75, no. 15, p. 6737-6747, 2001. https://doi.org/10.1128/jvi.75.15.6737-6747.2001
[3] A. Hall and K. Alexander, "Rna interference of human papillomavirus type 18 e6 and e7 induces senescence in hela cells", Journal of Virology, vol. 77, no. 10, p. 6066-6069, 2003. https://doi.org/10.1128/jvi.77.10.6066-6069.2003
[4] S. Duensing and K. Münger, "Human papillomavirus type 16 e7 oncoprotein can induce abnormal centrosome duplication through a mechanism independent of inactivation of retinoblastoma protein family members", Journal of Virology, vol. 77, no. 22, p. 12331-12335, 2003. https://doi.org/10.1128/jvi.77.22.12331-12335.2003
[5] T. Prathapam, C. Kühne, & L. Banks, "The hpv-16 e7 oncoprotein binds skip and suppresses its transcriptional activity", Oncogene, vol. 20, no. 52, p. 7677-7685, 2001. https://doi.org/10.1038/sj.onc.1204960
[6] M. Giarrè, S. Caldeira, I. Malanchi, F. Ciccolini, M. Leão, & M. Tommasino, "Induction of prb degradation by the human papillomavirus type 16 e7 protein is essential to efficiently overcome p16 ink4a-imposed g1 cell cycle arrest", Journal of Virology, vol. 75, no. 10, p. 4705-4712, 2001. https://doi.org/10.1128/jvi.75.10.4705-4712.2001
[7] H. Yun, M. Kim, H. Lee, W. Kim, J. Shin, H. Kimet al., "Structural basis for recognition of the tumor suppressor protein ptpn14 by the oncoprotein e7 of human papillomavirus", Plos Biology, vol. 17, no. 7, p. e3000367, 2019. https://doi.org/10.1371/journal.pbio.3000367
[8] C. Bello-Rios, S. Montaño, O. Garibay-Cerdenares, L. Araujo-Arcos, M. Leyva-Vázquez, & B. Illades-Aguiar, "Modeling and molecular dynamics of the 3d structure of the hpv16 e7 protein and its variants",, 2020. https://doi.org/10.20944/preprints202012.0671.v1
[9] L. Chemes, I. Sánchez, C. Smal, & G. Prat‐Gay, "Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein", Febs Journal, vol. 277, no. 4, p. 973-988, 2010. https://doi.org/10.1111/j.1742-4658.2009.07540.x
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Would you have the recipe for the Tris buffer that you could share? If not, the recipe can you share the molarity and the pH of the Tris buffer?
I'm wondering exactly how to resuspend the protein.
You mentioned the instructions as the following:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%.
I could use it as reference.
But I ordered 0.02mg, if I wanted to reconstitute to 1mg/mL, I would add 20ug sterile water, right?
If I plan to store the protein with 50% glycerol, would I actually resuspend with 10uL sterile water, and 10uL glycerol (for the 1mg/mL concentration?
If you want to get the protein with the final concentration of 0.1 mg/ml, you can refer to the following methods for reconstitution.
Reconstitute the protein completely with 100ul sterile water, and then add 100ul glycerol solution, with the final protein concentration of 0.1mg/ml.
The protein contains 50% glycerol and can be stored at -20℃/-80℃ for a long time.
Please address the final endotoxin level after producing. We like to know EU/ug.
We can provide free endotoxin removal service and guarantee endotoxin level within 0.1 EU/ug (1EU / ug).
KEGG: vg:1489079