Electroporation | Eppendorf Eporator
The Eppendorf Eporator is a compact instrument designed for fast and controlled electroporation of bacteria, yeasts and other micro-organisms. The instrument is unique due to its intuitive operation and user-friendly programming of standard methods, as well as its USB port where experimental data can be easily exported and documented. Electroporation using the Eppendorf Eporator yields higher transformation efficiencies than chemical transformations. Using electroporation can reduce time consumption and errors when buffers need to be prepared by the user.
Transformation of bacteria, yeasts and other micro-organisms.
- Faster sample handling- simple one button operation
- Intuitive use
- Fast and freely programmable-two program buttons allow storage and recall of most commonly used parameters.
- Safe electronics and integrated electroporation chamber eliminates voltage leaks and misuse
- Compact, space saving design for easy storage and transport
- Easy, GLP-compliant documentation via USB port
- Eporator for bacteria and yeast
- Electroporation buffers.
- Fusion chambers.
Preventative Maintenance and Service Level Agreements
- 1 year
- 2 year
- 3 year
Published Research Utilising the Eppendorf Eporator
- Durand, F. et al. (2012). Bilirubin oxidase from Bacillus pumilus: A promising enzyme for the elaboration of efficient cathodes in biofuel cells. Biosensors and Bioelectronics, vol 35, no 1, pp. 140-146. | http://www.sciencedirect.com/science/article/pii/S0956566312001121
- Lebedeva, M. et al. (2015). Initiation of spontaneous tumors in radish (Raphanus sativus): Cellular, molecular and physiological events. Journal of Plant Physiology, vol 173, pp. 97-104. | http://www.sciencedirect.com/science/article/pii/S0176161714002582
- Liu, Y. et al. (2014). Enhanced Activity of Rhizomucor miehei Lipase by Deglycosylation of Its Propeptide in Pichia pastoris. Current Microbiology, vol. 68, no 2, 186-191. | http://link.springer.com/article/10.1007/s00284-013-0460-0
- Simons, J. et al. (2013). Site directed immobilization of glucose-6-phosphate dehydrogenase via thiol-disulfide interchange: Influence on catalytic activity of cysteines introduced at different positions. Journal of Biotechnology, vol. 167, no 1, pp 1-7. | http://www.sciencedirect.com/science/article/pii/S0168165613002502
- Wang, T. et al. (2014). Enhanced expression of an industry applicable CotA laccase from Bacillus subtilis in Pichia pastoris by non-repressing carbon sources together with pH adjustment: Recombinant enzyme characterization and dye decolorization. Process Biochemistry, doi:10.1016/j.procbio.2014.10.009. | http://www.sciencedirect.com/science/article/pii/S1359511314005315