Blood Vessel Tissue Homogenizer & Homogenization Protocol

Ideal for Blood Vessel Tissue Homogenization

Do you spend lots of time and effort homogenizing blood vessel 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 a blood vessel tissue homogenization protocol.

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 blood vessel 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. The “Blue” model comes with a fan to maintain ambient temperatures, and the “Gold” model comes with a dry ice compartment to keep your samples at 4°C.
  • Easy and Convenient to Use
    Just place beads and buffer along with your blood vessel 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 Homogenization Protocol for Blood Vessel Tissue

Sample size

See the Protocol
microcentrifuge tube model (up to 300 mg) Small blood vessel samples
5mL tube model (100mg – 1g) Medium blood vessel samples

 

Selected Publications for Blood Vessel Samples

See all of our Bullet Blender publications!

Adamo, R. F., Fishbein, I., Zhang, K., Wen, J., Levy, R. J., Alferiev, I. S., & Chorny, M. (2016). Magnetically enhanced cell delivery for accelerating recovery of the endothelium in injured arteries. Journal of Controlled Release, 222, 169–175. https://doi.org/10.1016/j.jconrel.2015.12.025
Papke, C. L., Tsunezumi, J., Ringuette, L.-J., Nagaoka, H., Terajima, M., Yamashiro, Y., Urquhart, G., Yamauchi, M., Davis, E. C., & Yanagisawa, H. (2015). Loss of fibulin-4 disrupts collagen synthesis and maturation: implications for pathology resulting from EFEMP2 mutations. Human Molecular Genetics, 24(20), 5867–5879. https://doi.org/10.1093/hmg/ddv308
Reho, J. J., Zheng, X., Asico, L. D., & Fisher, S. A. (2015). Redox signaling and splicing dependent change in myosin phosphatase underlie early versus late changes in NO vasodilator reserve in a mouse LPS model of sepsis. American Journal of Physiology - Heart and Circulatory Physiology, 308(9), H1039–H1050. https://doi.org/10.1152/ajpheart.00912.2014
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
Rotllan, N., Chamorro-Jorganes, A., Araldi, E., Wanschel, A. C., Aryal, B., Aranda, J. F., Goedeke, L., Salerno, A. G., Ramirez, C. M., Sessa, W. C., Suarez, Y., & Fernandez-Hernando, C. (2015). Hematopoietic Akt2 deficiency attenuates the progression of atherosclerosis. The FASEB Journal, 29(2), 597–610. https://doi.org/10.1096/fj.14-262097
Carlström, M., Liu, M., Yang, T., Zollbrecht, C., Huang, L., Peleli, M., Borniquel, S., Kishikawa, H., Hezel, M., Persson, A. E. G., Weitzberg, E., & Lundberg, J. O. (2015). Cross-talk Between Nitrate-Nitrite-NO and NO Synthase Pathways in Control of Vascular NO Homeostasis. Antioxidants & Redox Signaling, 23(4), 295–306. https://doi.org/10.1089/ars.2013.5481
Liu, M., Zollbrecht, C., Peleli, M., Lundberg, J. O., Weitzberg, E., & Carlström, M. (2015). Nitrite-mediated renal vasodilatation is increased during ischemic conditions via cGMP-independent signaling. Free Radical Biology and Medicine, 84, 154–160. https://doi.org/10.1016/j.freeradbiomed.2015.03.025
Hao, P., Ren, Y., Pasterkamp, G., Moll, F. L., de Kleijn, D. P. V., & Sze, S. K. (2014). Deep proteomic profiling of human carotid atherosclerotic plaques using multidimensional LC-MS/MS. PROTEOMICS - Clinical Applications, 8(7–8), 631–635. https://doi.org/10.1002/prca.201400007
Chorny, M., Fishbein, I., Tengood, J. E., Adamo, R. F., Alferiev, I. S., & Levy, R. J. (2013). Site-specific gene delivery to stented arteries using magnetically guided zinc oleate-based nanoparticles loaded with adenoviral vectors. The FASEB Journal, 27(6), 2198–2206. https://doi.org/10.1096/fj.12-224659
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
Kuang, S.-Q., Kwartler, C. S., Byanova, K. L., Pham, J., Gong, L., Prakash, S. K., Huang, J., Kamm, K. E., Stull, J. T., Sweeney, H. L., & Milewicz, D. M. (2012). Rare, Nonsynonymous Variant in the Smooth Muscle-Specific Isoform of Myosin Heavy Chain, MYH11, R247C, Alters Force Generation in the Aorta and Phenotype of Smooth Muscle Cells. Circulation Research, 110(11), 1411–1422. https://doi.org/10.1161/CIRCRESAHA.111.261743
Fox, K. A., Longo, M., Tamayo, E., Gamble, P., Makhlouf, M., Mateus, J. F., & Saade, G. R. (2012). Sex-specific effects of nicotine exposure on developmental programming of blood pressure and vascular reactivity in the C57Bl/6J mouse. American Journal of Obstetrics and Gynecology, 207(3), 208.e1-208.e9. https://doi.org/10.1016/j.ajog.2012.06.021
Kassan, M., Galan, M., Partyka, M., Trebak, M., & Matrougui, K. (2011). Interleukin-10 Released by CD4+CD25+ Natural Regulatory T Cells Improves Microvascular Endothelial Function Through Inhibition of NADPH Oxidase Activity in Hypertensive Mice. Arteriosclerosis, Thrombosis, and Vascular Biology, 31(11), 2534–2542. https://doi.org/10.1161/ATVBAHA.111.233262
Shai, S.-Y., Sukhanov, S., Higashi, Y., Vaughn, C., Rosen, C. J., & Delafontaine, P. (2011). Low circulating insulin-like growth factor I increases atherosclerosis in ApoE-deficient mice. AJP: Heart and Circulatory Physiology, 300(5), H1898–H1906. https://doi.org/10.1152/ajpheart.01081.2010
Fox, K. A., Longo, M., Tamayo, E., Kechichian, T., Bytautiene, E., Hankins, G. D. V., Saade, G. R., & Costantine, M. M. (2011). Effects of pravastatin on mediators of vascular function in a mouse model of soluble Fms-like tyrosine kinase-1–induced preeclampsia. American Journal of Obstetrics and Gynecology, 205(4), 366.e1-366.e5. https://doi.org/10.1016/j.ajog.2011.06.083
Lee, Y. W., Lee, W. H., & Kim, P. H. (2010). Role of NADPH oxidase in interleukin-4-induced monocyte chemoattractant protein-1 expression in vascular endothelium. Inflammation Research, 59(9), 755–765. https://doi.org/10.1007/s00011-010-0187-3
Lee, Y. W., Lee, W. H., & Kim, P. H. (2010). Oxidative mechanisms of IL-4-induced IL-6 expression in vascular endothelium. Cytokine, 49(1), 73–79. https://doi.org/10.1016/j.cyto.2009.08.009
Hou, C. J.-Y., Tsai, C.-H., Su, C.-H., Wu, Y.-J., Chen, S.-J., Chiu, J.-J., Shiao, M.-S., & Yeh, H.-I. (2008). Diabetes Reduces Aortic Endothelial Gap Junctions in ApoE-deficient Mice: Simvastatin Exacerbates the Reduction. Journal of Histochemistry and Cytochemistry, 56(8), 745–752. https://doi.org/10.1369/jhc.2008.950816