Cell Culture

Ideal for Cell Culture Homogenization

Do you spend lots of time and effort homogenizing cell culture samples? The Bullet Blender® is a multi-sample homogenizer that delivers superior results. No other homogenizer comes close to delivering the Bullet Blender’s winning combination of top-quality performance and budget-friendly affordability.

The Bullet Blender® Homogenizer
Save Time, Effort and Get Superior Results

  • 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 cell culture samples – the sample tubes are kept closed during homogenization. There are no probes to clean between samples.
  • Samples Stay Cool Homogenizing causes only a few degrees of heating. Our “Blue” model comes with a fan to maintain ambient temperatures.
  • Easy and Convenient to Use Just place beads and buffer along with your cell culture sample in standard tubes, load tubes directly in the Bullet Blender, select time and speed, and press start.
  • Risk Free Purchase The Bullet Blender® comes with a 30 day money back guarantee and a 2 year warranty, with a 3 year warranty on the motor. The simple, reliable design enables the Bullet Blenders to sell for a fraction of the price of ultrasonic or other agitation based instruments, yet provides an easier, quicker technique.
Bullet Blender Homogenizer

Bullet Blender settings for Cell Culture Samples

Sample size

See the Protocol

microcentrifuge tube model (up to 300 mg) Small mammalian cell culture samples
5mL tube model (100mg – 1g) Medium mammalian cell culture samples
50mL tube model (100mg – 3.5g) Large mammalian cell culture samples
 

Selected publications for cell culture samples

See all of our Bullet Blender publications!

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
Clark, D. J., Mei, Y., Sun, S., Zhang, H., Yang, A. J., & Mao, L. (2016). Glycoproteomic Approach Identifies KRAS as a Positive Regulator of CREG1 in Non-small Cell Lung Cancer Cells. Theranostics, 6(1), 65–77. https://doi.org/10.7150/thno.12350
Tranchemontagne, Z. R., Camire, R. B., O’Donnell, V. J., Baugh, J., & Burkholder, K. M. (2016). Staphylococcus aureus Strain USA300 Perturbs Acquisition of Lysosomal Enzymes and Requires Phagosomal Acidification for Survival inside Macrophages. Infection and Immunity, 84(1), 241–253. https://doi.org/10.1128/IAI.00704-15
Wilde, A. D., Snyder, D. J., Putnam, N. E., Valentino, M. D., Hammer, N. D., Lonergan, Z. R., … Cassat, J. E. (2015). Bacterial Hypoxic Responses Revealed as Critical Determinants of the Host-Pathogen Outcome by TnSeq Analysis of Staphylococcus aureus Invasive Infection. PLOS Pathogens, 11(12), e1005341. https://doi.org/10.1371/journal.ppat.1005341
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
Dragunow, M., Feng, S., Rustenhoven, J., Curtis, M., & Faull, R. (2015). Studying Human Brain Inflammation in Leptomeningeal and Choroid Plexus Explant Cultures. Neurochemical Research. https://doi.org/10.1007/s11064-015-1682-2
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
Ran, L., Yu, Q., Zhang, S., Xiong, F., Cheng, J., Yang, P., … Wang, C.-Y. (2015). Cx3cr1 deficiency in mice attenuates hepatic granuloma formation during acute schistosomiasis by enhancing the M2-type polarization of macrophages. Disease Models & Mechanisms, 8(7), 691–700. https://doi.org/10.1242/dmm.018242
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
Behnia, F., Peltier, M. R., Saade, G. R., & Menon, R. (2015). Environmental Pollutant Polybrominated Diphenyl Ether, a Flame Retardant, Induces Primary Amnion Cell Senescence. American Journal of Reproductive Immunology, 74(5), 398–406. https://doi.org/10.1111/aji.12414
Ozgul, S., Kasap, M., Akpinar, G., Kanli, A., Güzel, N., Karaosmanoglu, K., … Iseri, P. (2015). Linking a compound-heterozygous Parkin mutant (Q311R and A371T) to Parkinson’s disease by using proteomic and molecular approaches. Neurochemistry International, 8586, 1–13. https://doi.org/10.1016/j.neuint.2015.03.007
Mouton, J., Loos, B., Moolman-Smook, J. C., & Kinnear, C. J. (2015). Ascribing novel functions to the sarcomeric protein, myosin binding protein H (MyBPH) in cardiac sarcomere contraction. Experimental Cell Research, 331(2), 338–351. https://doi.org/10.1016/j.yexcr.2014.11.006
Amidan, B. G., Orton, D. J., LaMarche, B. L., Monroe, M. E., Moore, R. J., Venzin, A. M., … Payne, S. H. (2014). Signatures for Mass Spectrometry Data Quality. Journal of Proteome Research, 13(4), 2215–2222. https://doi.org/10.1021/pr401143e
Da-Rè, C., Franzolin, E., Biscontin, A., Piazzesi, A., Pacchioni, B., Gagliani, M. C., … Costa, R. (2014). Functional Characterization of d rim2 , the Drosophila melanogaster Homolog of the Yeast Mitochondrial Deoxynucleotide Transporter. Journal of Biological Chemistry, 289(11), 7448–7459. https://doi.org/10.1074/jbc.M113.543926
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