Ideal for Muscle Tissue Homogenization

Do you spend lots of time and effort homogenizing muscle tissue 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 muscle tissue 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 muscle tissue 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 Muscle tissue

Sample size

See the Protocol

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

Selected publications for Muscle tissue

See all of our Bullet Blender publications!

Ohana, D., Dalebout, H., Marissen, R. J., Wulff, T., Bergquist, J., Deelder, A. M., & Palmblad, M. (2016). Identification of meat products by shotgun spectral matching. Food Chemistry, 203, 28–34. https://doi.org/10.1016/j.foodchem.2016.01.138
Metzger, D. C. H., Hemmer-Hansen, J., & Schulte, P. M. (2016). Conserved structure and expression of hsp70 paralogs in teleost fishes. Comparative Biochemistry and Physiology Part D: Genomics and Proteomics, 18, 10–20. https://doi.org/10.1016/j.cbd.2016.01.007
Bouley, R., Ding, D., Peng, Z., Bastian, M., Lastochkin, E., Song, W., … Chang, M. (2016). Structure–Activity Relationship for the 4(3H)-Quinazolinone Antibacterials. Journal of Medicinal Chemistry, 59(10), 5011–5021. https://doi.org/10.1021/acs.jmedchem.6b00372
Luethy, L. N., Erickson, A. K., Jesudhasan, P. R., Ikizler, M., Dermody, T. S., & Pfeiffer, J. K. (2016). Comparison of three neurotropic viruses reveals differences in viral dissemination to the central nervous system. Virology, 487, 1–10. https://doi.org/10.1016/j.virol.2015.09.019
Albury-Warren, T. M., Pandey, V., Spinel, L. P., Masternak, M., & Altomare, D. A. (2015). Prediabetes linked to excess glucagon in transgenic mice with pancreatic active AKT1. Journal of Endocrinology, JOE-15-0288. https://doi.org/10.1530/JOE-15-0288
Larsen, F. J., Schiffer, T. A., Ortenblad, N., Zinner, C., Morales-Alamo, D., Willis, S. J., … Boushel, R. (2015). High-intensity sprint training inhibits mitochondrial respiration through aconitase inactivation. The FASEB Journal. https://doi.org/10.1096/fj.15-276857
An, C., Bhetwal, B. P., Sanders, K. M., Somlyo, A. V., & Perrino, B. A. (2015). Role of Telokin in Regulating Murine Gastric Fundus Smooth Muscle Tension. PLOS ONE, 10(8), e0134876. https://doi.org/10.1371/journal.pone.0134876
Hurley-Sanders, J. L., Levine, J. F., Nelson, S. A. C., Law, J. M., Showers, W. J., & Stoskopf, M. K. (2015). Key metabolites in tissue extracts of Elliptio complanata identified using 1H nuclear magnetic resonance spectroscopy. Conservation Physiology, 3(1), cov023-cov023. https://doi.org/10.1093/conphys/cov023
Moore, C. D., Fahlman, A., Crocker, D. E., Robbins, K. A., & Trumble, S. J. (2015). The degradation of proteins in pinniped skeletal muscle: viability of post-mortem tissue in physiological research. Conservation Physiology, 3(1), cov019-cov019. https://doi.org/10.1093/conphys/cov019
Vechetti-Junior, I. J., Bertaglia, R. S., Fernandez, G. J., de Paula, T. G., de Souza, R. W. A., Moraes, L. N., … Dal-Pai-Silva, M. (2015). Aerobic Exercise Recovers Disuse-induced Atrophy Through the Stimulus of the LRP130/PGC-1 Complex in Aged Rats. The Journals of Gerontology Series A: Biological Sciences and Medical Sciences. https://doi.org/10.1093/gerona/glv064
Lynch, C. J., Xu, Y., Hajnal, A., Salzberg, A. C., & Kawasawa, Y. I. (2015). RNA Sequencing Reveals a Slow to Fast Muscle Fiber Type Transition after Olanzapine Infusion in Rats. PLOS ONE, 10(4), e0123966. https://doi.org/10.1371/journal.pone.0123966
Zheng, X., Reho, J. J., Wirth, B., & Fisher, S. A. (2015). TRA2β controls Mypt1 exon 24 splicing in the developmental maturation of mouse mesenteric artery smooth muscle. American Journal of Physiology - Cell Physiology, 308(4), C289–C296. https://doi.org/10.1152/ajpcell.00304.2014
Doldur-Balli, F., Ozel, M. N., Gulsuner, S., Tekinay, A. B., Ozcelik, T., Konu, O., & Adams, M. M. (2015). Characterization of a novel zebrafish (Danio rerio) gene, wdr81, associated with cerebellar ataxia, mental retardation and dysequilibrium syndrome (CAMRQ). BMC Neuroscience, 16(1). https://doi.org/10.1186/s12868-015-0229-4
Frank, P., Andersson, E., Pontén, M., Ekblom, B., Ekblom, M., & Sahlin, K. (2015). Strength training improves muscle aerobic capacity and glucose tolerance in elderly: Strength training in elderly. Scandinavian Journal of Medicine & Science in Sports, n/a-n/a. https://doi.org/10.1111/sms.12537
Psilander, N., Frank, P., Flockhart, M., & Sahlin, K. (2015). Adding strength to endurance training does not enhance aerobic capacity in cyclists: Concurrent training mitochondrial biogenesis. Scandinavian Journal of Medicine & Science in Sports, 25(4), e353–e359. https://doi.org/10.1111/sms.12338
Neishabouri, S. H., Hutson, S. M., & Davoodi, J. (2015). Chronic activation of mTOR complex 1 by branched chain amino acids and organ hypertrophy. Amino Acids, 47(6), 1167–1182. https://doi.org/10.1007/s00726-015-1944-y
Alves, R. D. A. M., Dane, A. D., Harms, A., Strassburg, K., Seifar, R. M., Verdijk, L. B., … Vreeken, R. J. (2015). Global profiling of the muscle metabolome: method optimization, validation and application to determine exercise-induced metabolic effects. Metabolomics, 11(2), 271–285. https://doi.org/10.1007/s11306-014-0701-7
Mootz, J. M., Benson, M. A., Heim, C. E., Crosby, H. A., Kavanaugh, J. S., Dunman, P. M., … Horswill, A. R. (2015). Rot is a key regulator of Staphylococcus aureus biofilm formation: Rot regulates S . aureus biofilm formation. Molecular Microbiology, 96(2), 388–404. https://doi.org/10.1111/mmi.12943
Tomechko, S. E., Liu, G., Tao, M., Schlatzer, D., Powell, C. T., Gupta, S., … Daneshgari, F. (2015). Tissue Specific Dysregulated Protein Subnetworks in Type 2 Diabetic Bladder Urothelium and Detrusor Muscle. Molecular & Cellular Proteomics, 14(3), 635–645. https://doi.org/10.1074/mcp.M114.041863
Do, A., Menon, V., Zhi, X., Gesing, A., Wiesenborn, D., Spong, A., … Masternak, M. M. (2015). Thyroxine modifies the effects of growth hormone in Ames dwarf mice. Aging (Albany, NY), 7(4), 241–255. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4429089/
Piórkowska, K., Nowak, J., Połtowicz, K., Ropka-Molik, K., & Szmatoła, T. (2015). Effect of newly found polymorphisms in the promoter region of the CAPN1 gene on transcript abundance in broiler chicken breast muscle. Animal Science Papers and Reports, 33(3), 287–298.
Psilander, N. (2014, December 19). The effect of different exercise regimens on mitochondrial biogenesis and performance. Karolinska Instituet. Retrieved from https://openarchive.ki.se/xmlui/bitstream/handle/10616/42310/Thesis_Niklas_Psilander.pdf?sequence=3
Drake, J. C., Bruns, D. R., Peelor, F. F., Biela, L. M., Miller, R. A., Hamilton, K. L., & Miller, B. F. (2014). Long-lived crowded-litter mice have an age-dependent increase in protein synthesis to DNA synthesis ratio and mTORC1 substrate phosphorylation. AJP: Endocrinology and Metabolism, 307(9), E813–E821. https://doi.org/10.1152/ajpendo.00256.2014
Moore, C. D., Crocker, D. E., Fahlman, A., Moore, M. J., Willoughby, D. S., Robbins, K. A., … Trumble, S. J. (2014). Ontogenetic changes in skeletal muscle fiber type, fiber diameter and myoglobin concentration in the Northern elephant seal (Mirounga angustirostris). Frontiers in Physiology, 5. https://doi.org/10.3389/fphys.2014.00217
King, I. N., Yartseva, V., Salas, D., Kumar, A., Heidersbach, A., Ando, D. M., … Ivey, K. N. (2014). The RNA-binding Protein TDP-43 Selectively Disrupts MicroRNA-1/206 Incorporation into the RNA-induced Silencing Complex. Journal of Biological Chemistry, 289(20), 14263–14271. https://doi.org/10.1074/jbc.M114.561902
van der Plas-Duivesteijn, S. J., Mohammed, Y., Dalebout, H., Meijer, A., Botermans, A., Hoogendijk, J. L., … Palmblad, M. (2014). Identifying Proteins in Zebrafish Embryos Using Spectral Libraries Generated from Dissected Adult Organs and Tissues. Journal of Proteome Research, 13(3), 1537–1544. https://doi.org/10.1021/pr4010585
Verhaart, I. E. C., van Vliet-van den Dool, L., Sipkens, J. A., de Kimpe, S. J., Kolfschoten, I. G. M., van Deutekom, J. C. T., … Aartsma-Rus, A. (2014). The Dynamics of Compound, Transcript, and Protein Effects After Treatment With 2OMePS Antisense Oligonucleotides in mdx Mice. Molecular Therapy—Nucleic Acids, 3(2), e148. https://doi.org/10.1038/mtna.2014.1
Mathewson, M. A., Chambers, H. G., Girard, P. J., Tenenhaus, M., Schwartz, A. K., & Lieber, R. L. (2014). Stiff muscle fibers in calf muscles of patients with cerebral palsy lead to high passive muscle stiffness: CP CALF MUSCLE FIBER STIFFNESS. Journal of Orthopaedic Research, 32(12), 1667–1674. https://doi.org/10.1002/jor.22719
Lashgari, M., & Lee, H. K. (2014). Determination of perfluorinated carboxylic acids in fish fillet by micro-solid phase extraction, followed by liquid chromatography–triple quadrupole mass spectrometry. Journal of Chromatography A, 1369, 26–32. https://doi.org/10.1016/j.chroma.2014.09.082
Mukund, K., Mathewson, M., Minamoto, V., Ward, S. R., Subramaniam, S., & Lieber, R. L. (2014). Systems analysis of transcriptional data provides insights into muscle’s biological response to botulinum toxin: Transcriptional Profiling after BoNT-A. Muscle & Nerve, 50(5), 744–758. https://doi.org/10.1002/mus.24211
Menon, V., Zhi, X., Hossain, T., Bartke, A., Spong, A., Gesing, A., & Masternak, M. M. (2014). The contribution of visceral fat to improved insulin signaling in Ames dwarf mice. Aging Cell, 13(3), 497–506. https://doi.org/10.1111/acel.12201
Melero, M., García-Párraga, D., Corpa, J., Ortega, J., Rubio-Guerri, C., Crespo, J., … Sánchez-Vizcaíno, J. (2014). First molecular detection and characterization of herpesvirus and poxvirus in a Pacific walrus (Odobenus rosmarus divergens). BMC Veterinary Research, 10(1), 968. https://doi.org/10.1186/s12917-014-0308-2
Schuh, R. A., Jackson, K. C., Schlappal, A. E., Spangenburg, E. E., Ward, C. W., Park, J. H., … Fishman, P. S. (2014). Mitochondrial oxygen consumption deficits in skeletal muscle isolated from an Alzheimer’s disease-relevant murine model. BMC Neuroscience, 15(1), 24. https://doi.org/10.1186/1471-2202-15-24
Drake, J. C., Peelor, F. F., Biela, L. M., Watkins, M. K., Miller, R. A., Hamilton, K. L., & Miller, B. F. (2013). Assessment of Mitochondrial Biogenesis and mTORC1 Signaling During Chronic Rapamycin Feeding in Male and Female Mice. The Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 68(12), 1493–1501. https://doi.org/10.1093/gerona/glt047
Erickson, A. K., & Pfeiffer, J. K. (2013). Dynamic Viral Dissemination in Mice Infected with Yellow Fever Virus Strain 17D. Journal of Virology, 87(22), 12392–12397. https://doi.org/10.1128/JVI.02149-13
Cheng, X., Guo, S., Liu, Y., Chu, H., Hakimi, P., Berger, N. A., … Kao, H.-Y. (2013). Ablation of Promyelocytic Leukemia Protein (PML) Re-patterns Energy Balance and Protects Mice from Obesity Induced by a Western Diet. Journal of Biological Chemistry, 288(41), 29746–29759. https://doi.org/10.1074/jbc.M113.487595
Miller, B. F., Robinson, M. M., Reuland, D. J., Drake, J. C., Peelor, F. F., Bruss, M. D., … Hamilton, K. L. (2013). Calorie Restriction Does Not Increase Short-term or Long-term Protein Synthesis. The Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 68(5), 530–538. https://doi.org/10.1093/gerona/gls219
Mcgowan, I., Hoesley, C., Cranston, R. D., Andrew, P., Janocko, L., Dai, J. Y., … Mayer, K. (2013). A Phase 1 Randomized, Double Blind, Placebo Controlled Rectal Safety and Acceptability Study of Tenofovir 1% Gel (MTN-007). PLoS ONE, 8(4), e60147. https://doi.org/10.1371/journal.pone.0060147
Moghadaszadeh, B., Rider, B. E., Lawlor, M. W., Childers, M. K., Grange, R. W., Gupta, K., … Beggs, A. H. (2013). Selenoprotein N deficiency in mice is associated with abnormal lung development. The FASEB Journal, 27(4), 1585–1599. https://doi.org/10.1096/fj.12-212688
Gao, N., Huang, J., He, W., Zhu, M., Kamm, K. E., & Stull, J. T. (2013). Signaling through Myosin Light Chain Kinase in Smooth Muscles. Journal of Biological Chemistry, 288(11), 7596–7605. https://doi.org/10.1074/jbc.M112.427112
Hanke, M. L., Heim, C. E., Angle, A., Sanderson, S. D., & Kielian, T. (2013). Targeting Macrophage Activation for the Prevention and Treatment of Staphylococcus aureus Biofilm Infections. The Journal of Immunology, 190(5), 2159–2168. https://doi.org/10.4049/jimmunol.1202348
Frank, P., Katz, A., Andersson, E., & Sahlin, K. (2013). Acute exercise reverses starvation-mediated insulin resistance in humans. AJP: Endocrinology and Metabolism, 304(4), E436–E443. https://doi.org/10.1152/ajpendo.00416.2012
Percival, J. M., Siegel, M. P., Knowels, G., & Marcinek, D. J. (2013). Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition. Human Molecular Genetics, 22(1), 153–167. https://doi.org/10.1093/hmg/dds415
Riisager, M., Duno, M., Hansen, F. J., Krag, T. O., Vissing, C. R., & Vissing, J. (2013). A new mutation of the fukutin gene causing late-onset limb girdle muscular dystrophy. Neuromuscular Disorders, 23(7), 562–567. https://doi.org/10.1016/j.nmd.2013.04.006
Brault, J. J., Pizzimenti, N. M., Dentel, J. N., & Wiseman, R. W. (2013). Selective inhibition of ATPase activity during contraction alters the activation of p38 MAP kinase isoforms in skeletal muscle. Journal of Cellular Biochemistry, 114(6), 1445–1455. https://doi.org/10.1002/jcb.24486
Veltrop, M., van der Kaa, J., Claassens, J., van Vliet, L., Verbeek, S., & Aartsma-Rus, A. (2013). Generation of Embryonic Stem Cells and Mice for Duchenne Research. PLoS Currents. https://doi.org/10.1371/currents.md.cbf1d33001de80923ce674302cad7925
Liu, B.-H., Lin, Y.-Y., Wang, Y.-C., Huang, C.-W., Chen, C.-C., Wu, S.-C., … Ding, S.-T. (2013). Porcine Adiponectin Receptor 1 Transgene Resists High-fat/Sucrose Diet-Induced Weight Gain, Hepatosteatosis and Insulin Resistance in Mice. Experimental Animals, 62(4), 347–360. https://doi.org/10.1538/expanim.62.347
Chaker, B., Samra, T. A., Datta, N. S., & Abou-Samra, A. B. (2013). Altered Responses to Cold Environment in Urocortin 1 and Corticotropin-Releasing Factor Deficient Mice. Physiology Journal, 2013, 1–7. https://doi.org/10.1155/2013/185767
Battaglia, G. M., Zheng, D., Hickner, R. C., & Houmard, J. A. (2012). Effect of exercise training on metabolic flexibility in response to a high-fat diet in obese individuals. AJP: Endocrinology and Metabolism, 303(12), E1440–E1445. https://doi.org/10.1152/ajpendo.00355.2012
Hecker, P. A., Mapanga, R. F., Kimar, C. P., Ribeiro, R. F., Brown, B. H., O’Connell, K. A., … Stanley, W. C. (2012). Effects of glucose-6-phosphate dehydrogenase deficiency on the metabolic and cardiac responses to obesogenic or high-fructose diets. AJP: Endocrinology and Metabolism, 303(8), E959–E972. https://doi.org/10.1152/ajpendo.00202.2012
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