Muscle Tissue Homogenizer & Homogenization Protocol

Ideal for Muscle Tissue Homogenization

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

Muscle Tissue Homogenization Protocol

Sample size

See the Protocol
microcentrifuge tube model (up to 300 mg) Small brain samples
5mL tube model (100mg - 1g) Medium brain samples
50mL tube model (100mg - 3.5g) Large brain samples

What Else Can You Homogenize? Tough or Soft, No Problem! 

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.

the Bullet Blender high-throughput tissue homogenizer

Muscle tissue pieces (on beads in upper photo) are completely homogenized into the buffer (slightly darker in lower photo). 

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    Bullet Blender Models

    Select Publications using the Bullet Blender to Homogenize Muscle Tissue

    See all of our Bullet Blender publications!

    Sarasamma, S., Audira, G., Juniardi, S., Sampurna, B., Lai, Y.-H., Hao, E., Chen, J.-R., & Hsiao, C.-D. (2018). Evaluation of the Effects of Carbon 60 Nanoparticle Exposure to Adult Zebrafish: A Behavioral and Biochemical Approach to Elucidate the Mechanism of Toxicity. International Journal of Molecular Sciences, 19(12), 3853. https://doi.org/10.3390/ijms19123853
    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., Suckow, M. A., Schroeder, V. A., Wolter, W. R., Mobashery, S., & 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., Calbet, J. A., Holmberg, H.-C., & 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., Mareco, E. A., de Freitas, C. E. A., Aguiar, A. F., Carvalho, R. F., & 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., Kersten, S., Berger, R., Hankemeier, T., & 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., Kielian, T., Torres, V. J., & 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., Chance, M. R., & 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., Sun, L., Bartke, A., & Masternak, M. M. (2015). Thyroxine modifies the effects of growth hormone in Ames dwarf mice. Aging (Albany, NY), 7(4), 241–255. 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). The effect of different exercise regimens on mitochondrial biogenesis and performance [Karolinska Instituet]. 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., Kanatous, S. B., & 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., Stallings, N. R., Elliott, J. L., Srivastava, D., & 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., Henneman, A. A., Deelder, A. M., Spaink, H. P., & 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., Liefaard, L., Ridings, J. E., Hood, S. R., & 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., Rivera-Arroyo, B., & 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., Dugger, N., Shi, G., & 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., Hanson, R. W., & 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., Hellerstein, M. K., & 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., Carballo-Dieguez, A., Ayudhya, R. K. N., Piper, J., Hladik, F., & 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., Boukedes, S. S., Owen, C. A., & 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., Mersmann, H. J., Cheng, W. T. K., & 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

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