Ideal for Cell Culture Homogenization
Do you spend lots of time and effort homogenizing cultured cells? 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 cultured 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.Cultured Cells Homogenization Protocol
Sample size |
See the Protocol |
| microcentrifuge tube model (up to 300 mg) | Small cell culture samples |
| 5mL tube model (100mg - 1g) | Medium cell culture samples |
| 50mL tube model (100mg - 3.5g) | Large cell culture 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.
Want more guidance? Need a quote? Contact us:
Bullet Blender Models
Select Publications using the Bullet Blender to Homogenize Cultured Cells
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., Hinger, S. A., Aysanoa, E. E., Blanchard, C., Dunman, P. M., Wasserman, G. A., Chen, J., Shopsin, B., Gilmore, M. S., Skaar, E. P., & 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., Xu, J.-F., Nie, H., Zhong, Q., Yang, X., Yang, F., Gong, Q., Kuczma, M., Kraj, P., Gu, W., Ren, B.-X., & 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., Baykal, A. T., & Iseri, P. (2015). Linking a compound-heterozygous Parkin mutant (Q311R and A371T) to Parkinson’s disease by using proteomic and molecular approaches. Neurochemistry International, 85–86, 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., Smith, R. D., Sego, L. H., Tardiff, M. F., & 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., Mazzotta, G., Tacchetti, C., Zordan, M. A., Zeviani, M., Bernardi, P., Bianchi, V., De Pittà, 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
