Ideal for Yeast Cells Homogenization
Do you spend lots of time and effort homogenizing yeast samples? The Bullet Blender® tissue homogenizer delivers high quality and superior yields. No other homogenizer comes close to delivering the Bullet Blender’s winning combination of top-quality performance and budget-friendly affordability. See below for a yeast cells homogenization protocol.
Save Time, Effort and Get Superior Results with
The Bullet Blender Homogenizer
Consistent and High Yield Results
Run up to 24 samples at the same time under microprocessor-controlled conditions, ensuring experimental reproducibility and high yield. Process samples from 10mg or less up to 3.5g.No Cross Contamination
No part of the Bullet Blender ever touches the tissue – the sample tubes are kept closed during homogenization. There are no probes to clean between samples.Samples Stay Cool
The Bullet Blenders’ innovative and elegant design provides convective cooling of the samples, so they do not heat up more than several degrees. In fact, our Gold+ models hold the sample temperature to about 4ºC.Easy and Convenient to Use
Just place beads and buffer along with your tissue sample in standard tubes, load tubes directly in the Bullet Blender, select time and speed, and press start.Risk Free Purchase
Thousands of peer-reviewed journal articles attest to the consistency and quality of the Bullet Blender homogenizer. We offer a 2 year warranty, extendable to 4 years, because our Bullet Blenders are reliable and last for many years.Yeast Cells Homogenization Protocol
Sample size |
See the Protocol |
| microcentrifuge tube model (up to 300 mg) | Small yeast samples |
| 5mL tube model (100mg - 1g) | Medium yeast samples |
| 50mL tube model (100mg - 3.5g) | Large yeast samples |
What Else Can You Homogenize? Tough or Soft, No Problem!Â
The Bullet Blender can process a wide range of samples including organ tissue, cell culture, plant tissue, and small organisms. You can homogenize samples as tough as mouse femur or for gentle applications such as tissue dissociation or organelle isolation.
Yeast cells intact (in upper photo) are completely homogenized (in lower photo).Â
Want more guidance? Need a quote? Contact us:
Bullet Blender Models
Select Publications using the Bullet Blender to Homogenize Yeast Cells
Rasool, A., Ahmed, M. S., & Li, C. (2016). Overproduction of squalene synergistically downregulates ethanol production in Saccharomyces cerevisiae. Chemical Engineering Science, 152, 370–380. https://doi.org/10.1016/j.ces.2016.06.014
Orgil, O., Mor, H., Matityahu, A., & Onn, I. (2016). Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity. Nucleic Acids Research, gkw539. https://doi.org/10.1093/nar/gkw539
Shwartz, M., Matityahu, A., & Onn, I. (2016). Identification of Functional Domains in the Cohesin Loader Subunit Scc4 by a Random Insertion/Dominant Negative Screen. G3: Genes|Genomes|Genetics, g3.116.031674. https://doi.org/10.1534/g3.116.031674
Zheng, Y., Xie, J., Huang, X., Dong, J., Park, M. S., & Chan, W. K. (2016). Binding studies using Pichia pastoris expressed human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins. Protein Expression and Purification, 122, 72–81. https://doi.org/10.1016/j.pep.2016.02.011
Mashock, M. J. (2016). Examining mechanism of toxicity of copper oxide nanoparticles to Saccharomyces cerevisiae and Caenorhabditis elegans. Marquette University.
Avbelj, M., Zupan, J., Kranjc, L., & Raspor, P. (2015). Quorum-Sensing Kinetics in Saccharomyces cerevisiae : A Symphony of ARO Genes and Aromatic Alcohols. Journal of Agricultural and Food Chemistry, 63(38), 8544–8550. https://doi.org/10.1021/acs.jafc.5b03400
Meyer, R. E., Chuong, H. H., Hild, M., Hansen, C. L., Kinter, M., & Dawson, D. S. (2015). Ipl1/Aurora-B is necessary for kinetochore restructuring in meiosis I in Saccharomyces cerevisiae. Molecular Biology of the Cell, 26(17), 2986–3000. https://doi.org/10.1091/mbc.E15-01-0032
Aylward, F. O., Khadempour, L., Tremmel, D. M., McDonald, B. R., Nicora, C. D., Wu, S., Moore, R. J., Orton, D. J., Monroe, M. E., Piehowski, P. D., Purvine, S. O., Smith, R. D., Lipton, M. S., Burnum-Johnson, K. E., & Currie, C. R. (2015). Enrichment and Broad Representation of Plant Biomass-Degrading Enzymes in the Specialized Hyphal Swellings of Leucoagaricus gongylophorus, the Fungal Symbiont of Leaf-Cutter Ants. PLOS ONE, 10(8), e0134752. https://doi.org/10.1371/journal.pone.0134752
Desai, J., Cheng, S., Ying, T., Nguyen, M., Clancy, C., Lanni, F., & Mitchell, A. (2015). Coordination of Candida albicans Invasion and Infection Functions by Phosphoglycerol Phosphatase Rhr2. Pathogens, 4(3), 573–589. https://doi.org/10.3390/pathogens4030573
Zhang, L., Li, X., Hill, R. C., Qiu, Y., Zhang, W., Hansen, K. C., & Zhao, R. (2015). Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding. Nucleic Acids Research, 43(6), 3286–3297. https://doi.org/10.1093/nar/gkv062
Orgil, O., Matityahu, A., Eng, T., Guacci, V., Koshland, D., & Onn, I. (2015). A Conserved Domain in the Scc3 Subunit of Cohesin Mediates the Interaction with Both Mcd1 and the Cohesin Loader Complex. PLOS Genetics, 11(3), e1005036. https://doi.org/10.1371/journal.pgen.1005036
Kurtzman, C. P., & Robnett, C. J. (2014). Three new anascosporic genera of the Saccharomycotina: Danielozyma gen. nov., Deakozyma gen. nov. and Middelhovenomyces gen. nov. Antonie van Leeuwenhoek, 105(5), 933–942. https://doi.org/10.1007/s10482-014-0149-9
Wiedner, S. D., Ansong, C., Webb-Robertson, B.-J., Pederson, L. M., Fortuin, S., Hofstad, B. A., Shukla, A. K., Panisko, E. A., Smith, R. D., & Wright, A. T. (2013). Disparate Proteome Responses of Pathogenic and Nonpathogenic Aspergilli to Human Serum Measured by Activity-Based Protein Profiling (ABPP). Molecular & Cellular Proteomics, 12(7), 1791–1805. https://doi.org/10.1074/mcp.M112.026534
Wiedner, S. D., Burnum, K. E., Pederson, L. M., Anderson, L. N., Fortuin, S., Chauvigne-Hines, L. M., Shukla, A. K., Ansong, C., Panisko, E. A., Smith, R. D., & Wright, A. T. (2012). Multiplexed Activity-based Protein Profiling of the Human Pathogen Aspergillus fumigatus Reveals Large Functional Changes upon Exposure to Human Serum. Journal of Biological Chemistry, 287(40), 33447–33459. https://doi.org/10.1074/jbc.M112.394106
Yin, Y., Liu, Y., Jin, H., Wang, S., Zhao, S., Geng, X., Li, M., & Xu, F. (2012). Polyethylene glycol-mediated transformation of fused egfp-hph gene under the control of gpd promoter in Pleurotus eryngii. Biotechnology Letters, 34(10), 1895–1900. https://doi.org/10.1007/s10529-012-0985-5
Suzuki, Y., Murray, S. L., Wong, K. H., Davis, M. A., & Hynes, M. J. (2012). Reprogramming of carbon metabolism by the transcriptional activators AcuK and AcuM in Aspergillus nidulans: Transcription factors controlling carbon metabolism. Molecular Microbiology, 84(5), 942–964. https://doi.org/10.1111/j.1365-2958.2012.08067.x
