Dr Ruth Rose
Protein Facility Manager
Email: email@example.comTelephone: Office: +44 (0)20 7882 4620 Lab: +44 (0)20 7882 7603Room Number: Room 4.33/4.36, Fogg building
- I run the protein production facility.
- I offer a service for gene cloning and protein production and purification.
- If you have any questions regarding these techniques or if you’re stuck with your experiments, just ask.
- The facility has a sonicator, AKTApure and full range of gel tanks and western blotting equipment.
Protein Production Facility
I have run the Protein Production Facility for 10 years. It offers services for all stages of the purification process, from gene cloning and recombinant technology to the preparation of highly pure protein ready for crystallography with every step in between. The facility has also a speciality of purifying antibodies from secreted media. A range of specialist equipment is housed in the facility including an array of AKTA systems, variety of columns and sonicator. A number of expression systems are available including yeast and mammalian cells. Additional equipment includes a vacuum concentrator and western blotting.
For several years I have been involved in examining plastic biodegradation. I am developing new methods for assessing biodegradation in an artificial system that mimics the environment. I am particularly interested in the mechanism of polymer breakdown, leading towards polymer uptake and incorporation. This is a fast moving, emotive and challenging field but it is imperative that we make reasoned, rational decisions to ensure the best health of the planet.
I am a biochemist, a microbiologist, a geneticist and with a hint of polymer chemist. I have fantastic industrial collaborations that provide samples. QMUL and SBCS is ideally suited for this type of research as we are a fantastically diverse department allowing the transfer of ideas and samples from ecologists and environmental biologists to laboratory and theoretical scientists.
Publications from the Protein Production Facility
Younan, N.D., Chen, K.F., Rose, R.S., Crowther, D.C., Viles, J.H. (2018) Prion protein stabilizes amyloid- (A) oligomers and enhances A neurotoxicity in a Drosophila model of Alzheimer’s disease. JBC. 293: 13090-13099
Bridge, K. S., Shah, K. M., Li, Y., Foxler, D. E., Wong, S. C. K., Miller, D. C., Davidson, K. M., Foster, J. G., Rose, R., Hodgkinson, M. R., Ribeiro, P. S., Aboobaker, A. A., Yashiro, K., Wang, X., Graves, P. R., Plevin, M. J., Lagos, D., Sharp, T. V. (2017) Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins. Cell Reports. 20:173-187
Novoselova, T.V., Rose, R.S., Marks, H.M., Sullivan, J.A. (2013) SUMOylation regulates the Homologous to E6-AP Carboxy Terminus (HECT) ubiquitin ligase Rsp5p. JBC. 288: 10308-10317
Hamilton, M.L., Kuate, S.P., Brazier-Hicks, M., Caulfield, J.C., Rose, R., Edwards, R., Torto, B., Pickett, J.A., Hooper, A.M. (2012) Elucidation of the biosynthesis of the di-C-glycosylflavone isoschaftoside, an allelopathic component from Desmodium spp. that inhibits Striga spp. development. Phytochemistry. 84: 169-176
Waite, R.D., Rose, R.S., Rangarajan, M., Aduse-Opoku, J., Hashim, A., Curtis, M.A. (2012) Pseudomonas aeruginosa Possesses Two Putative Type I Signal Peptidases, LepB and PA1303, Each with Distinct Roles in Physiology and Virulence. Journal of Bacteriology. 194 (17): 4521-36
Novoselova, T.V., Zahira, K., Rose, R.S., Sullivan, J.A. (2012) Bul proteins, a nonredundant, antagonistic family of ubiquitin ligase regulatory proteins. Eukaryotic Cell. 11(4) 462-70
Hughes, M., Snetkov, V., Rose, R.-S., Trousil, S., Mermoud, J.E., Dingwall, C. (2010) Neurite-like structures induced by mevalonate pathway blockade are due to the stability of cell adhesion foci and are enhanced by the presence of APP. J. Neurochem. 114: 832-842
M.J. Warren, E. Deery and S. R. Rose (2009) Biosynthesis of Siroheme and Coenzyme F430. In M.J. Warren and A.G. Smith (Eds) Tetrapyrroles: Birth, life and Death (Molecular Biology Intelligence Unit) (Chp 22) Springer-Verlag: New York
Schroeder, S., Lawrence, A.D., Biedendieck, R., Rose, R.S., Deery, E., Graham, R.M., McLean, K.J., Munro, A.W., Rigby, S.E.J., Warren, M.J. (2008) Demonstration that CobG, the monooxygenase associated with the ring contraction process of the aerobic cobalamin (Vitamin B12) biosynthetic pathway, contains as Fe-S center and a mononuclear non-heme iron center. JBC. 284 (8) 4796-4805
Schubert, H.L., Rose, R.S., Leech, H.K., Brindley, A.A., Hill, C.P., Rigby, S.E.J., Warren, M.J. (2008) Structure and function of SirC from Bacillus megaterium: a metal-binding precorrin-2 dehydrogenase. Biochem J. 415: 257-263
Opalaye, O.*, Rose, R-S.*, Whittaker, M.M., Woo, E.-J., Whittaker, J.W. and R.W. Pickersgill. (2006) Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase. JBC. 281: 6428 – 6433 *joint authorship