Emulsiflex c5 homogenizer

Manufactured by Avestin

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About the product

The EmulsiFlex-C5 is a high-pressure homogenizer designed for the emulsification and dispersion of a wide range of materials. It is capable of generating pressures up to 30,000 psi (2,068 bar) to create stable emulsions and dispersions.

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Lab products found in correlation

Ni nta agarose, by Qiagen (7 mentions) Hispur ni nta resin, by Thermo Fisher Scientific (5 mentions) Pd 10 desalting column, by GE Healthcare (5 mentions) Egg phosphatidylcholine, by Lipoid (5 mentions) Complete edta free protease inhibitor cocktail, by Roche (4 mentions) Akta fplc, by GE Healthcare (4 mentions) Benzonase, by Merck Group (4 mentions) Ti45 rotor, by Beckman Coulter (4 mentions) Histrap column, by GE Healthcare (4 mentions) Akta prime fplc system, by GE Healthcare (4 mentions) Pgex 6p1 vector, by Thermo Fisher Scientific (3 mentions) Prescission protease, by GE Healthcare (3 mentions) Protease inhibitor cocktail tablet, by Roche (3 mentions) Ni nta bead, by Qiagen (3 mentions) Nickel chelating sepharose fast flow column, by GE Healthcare (3 mentions) Protease inhibitor cocktail, by Roche (3 mentions) Lysozyme, by Merck Group (3 mentions) Miglyol 812 n, by Sasol (3 mentions) Monoq 10 100 gl column, by GE Healthcare (3 mentions) Fiberlite f10 4x1000 lex carbon fiber rotor, by Thermo Fisher Scientific (3 mentions)

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Market Availability & Pricing

The EmulsiFlex-C5 homogenizer by Avestin is a laboratory-scale, high-pressure homogenizer designed for producing emulsions, dispersions, and nanoemulsions. It operates at adjustable pressures up to 30,000 psi, with a processing rate of 1–5 liters per hour, depending on the homogenizing pressure.

As of June 2025, the current commercial status of the EmulsiFlex-C5 is unclear. While some distributors list the product, there is no explicit confirmation of its availability on Avestin's official website or through official press releases. Therefore, we cannot confirm whether the EmulsiFlex-C5 is still actively commercialized.

In the absence of official pricing information, second-hand units have been observed on the market, suggesting that pre-owned EmulsiFlex-C5 homogenizers are available in the range of approximately $5,000 to €10,530.

For those seeking alternatives, Avestin's EmulsiFlex-C3 is a comparable model. It offers a consistent flow rate of 3 liters per hour, adjustable pressures up to 30,000 psi, and is suitable for temperature-sensitive products. The C3 features an electrically driven high-pressure pump, minimizing the need for compressed air or gas.

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Spelling variants (same manufacturer)

EmulsiFlex-C5 - 437 citations EmulsiFlex - 107 citations Emulsiflex C5 high-pressure homogenizer - 71 citations C5 homogenizer - 9 citations

The spelling variants listed below correspond to different ways the product may be referred to in scientific literature.
These variants have been automatically detected by our extraction engine, which groups similar formulations based on semantic similarity.

212 protocols using «emulsiflex c5 homogenizer»

Purification of Recombinant and Native Tubulins

2025

αE254Q-tubulin expression was induced by adding 3 ml of frozen BIICs per liter to a High Five insect cell culture grown to densities of ~1.2 × 10⁶ cells/ml. Cells were harvested 48 h post-infection by centrifugation (15 min, 900× g, 4 °C). Cell pellets were then washed with cold PBS, centrifuged again (15 min, 1000× g, 4 °C) and stored at −80 °C.
Recombinant human tubulin was purified following a previously described protocol^{31 ,56} using slightly modified buffers. Cell pellets obtained from 2 L of High Five insect cells expressing human TUBB3-TEVsite-StrepTagII, with the C-terminal StrepTagII cleavable by tobacco etch virus (TEV) protease, and TUBA1B-His, with internal 6x His-Tag (WT, αE254A, αE254N, and αE254Q) were resuspended 1:1 (vol/vol) in cold lysis buffer (80 mM PIPES, 1 mM EGTA, 1 mM MgCl₂, 50 mM imidazole, 100 mM KCl, 0.2 mM GTP, 1 mM β-ME, pH 7.2) and lysed using an Emulsiflex-C5 homogenizer (Avestin). The resulting lysate was clarified by ultracentrifugation (160,000× g, 45 min, 4 °C), filtered using 0.22 µm PES syringe filters (4602, Merck) and flowed through a 5-mL HisTrap HP column (GE17-5255-01, Cytiva). The column was then first washed with 5 column volumes (CVs) of Ni-dilution buffer (80 mM PIPES, 1 mM EGTA, 6 mM MgCl₂, 50 mM imidazole, 0.2 mM GTP, 1 mM β-ME, pH 7.2), then with 5 CVs of Ni wash buffer 1 (80 mM PIPES, 1 mM EGTA, 11 mM MgCl₂, 0.2 mM GTP, 5 mM ATP, 1 mM β-ME, pH 7.2), then with 5 CVs of Ni wash buffer 2 (80 mM PIPES, 1 mM EGTA, 5 mM MgCl₂, 0.1% (vol/vol) Tween-20, 10% (w/vol) glycerol), 0.2 mM GTP, 1 mM β-ME, pH 7.2) and finally with 5 CVs of Ni-dilution buffer. The protein was eluted with Ni-elution buffer (80 mM PIPES, 1 mM EGTA, 5 mM MgCl₂, 300 mM imidazole 0.2 mM GTP, 1 mM β-ME, pH 7.2). The eluted protein was collected in a 96-well plate containing 1 volume of Strep binding buffer (80 mM PIPES, 1 mM EGTA, 5 mM MgCl₂, 0.2 mM GTP, 1 mM β-ME, pH 7.2) in order to immediately dilute 4 times the imidazole present in the Ni-elution buffer. The eluted fractions corresponding to the main peak were joined, diluted 2 times with Strep binding buffer, and passed through two HiTrap SP FF columns of 1 mL (17505401, Cytiva) and one StrepTrap HP of 5 mL (28-9075-48, Cytiva) serially connected and equilibrated in Strep binding buffer. The columns were then washed with 2 CVs of Strep binding buffer, and the protein was eluted in Strep elution buffer (80 mM PIPES, 1 mM EGTA, 5 mM MgCl₂, 2.5 mM d-desthiobiotin, 0.2 mM GTP, 1 mM β-ME, pH 7.2). The eluted protein was supplemented with TEV protease at a ratio of 1:10 (1 mg of TEV protease per 10 mg of tubulin) and incubated for 2 h at 4 °C in order to remove the C-terminal Strep-Tag II from TUBB3. After the tag cleavage, the protein was centrifuged at 204,428× g, 10 min, 4 °C to remove possible aggregates and insoluble fractions. The supernatant was then passed through two 1 ml HiTrap SP FF columns of 1 mL (17505401,Cytiva) serially connected to the top of two HiPrep Desalting 26/10 desalting columns (17-5087-01, Cytiva) to remove the TEV protease and to equilibrate the protein in tubulin storage buffer (80 mM PIPES, 1 mM EGTA 1 mM MgCl₂, 0.2 mM GTP, pH 6.8). The tubulin-containing fractions were pooled, concentrated using Amicon Ultra-4, 50 kDa MWCO (Millipore) to a concentration higher than 5 mg/mL and ultracentrifuged (280,000× g, 10 min, 4 °C). The resulting clarified pure tubulin solution was aliquoted, snap-frozen, and stored in liquid nitrogen for next use.
Porcine brain tubulin was purified as previously described^{57 (link)}. Briefly, tubulin was purified from brain extract by sequential cycles of polymerization of tubulin at 37 °C in high-concentration PIPES buffer supplemented with ATP, GTP, and glycerol, followed by depolymerization on ice. For long-term storage 5-ml-tubulin aliquots were frozen and stored in liquid nitrogen. Tubulin used in experiments was passed through another polymerization/depolymerization cycle and was snap-frozen and stored in 10 µl aliquots in liquid nitrogen. Tubulin was labeled with CF640R-NHS (SCJ4600044, Merck) or biotin-NHS (203112, Merck), as previously described^{58 (link)}. Briefly, NHS-fluorophores dissolved in anhydrous DMSO were added drop by drop to microtubules obtained from cycled tubulin while gently mixing. After 40 min, the labeled microtubules were depolymerized at 4 °C. The samples were then ultracentrifuged (280,000× g, 10 min, 4 °C), and the pellet was discarded. The supernatant containing labeled tubulin was aliquoted, snap-frozen, and stored in liquid nitrogen in 5 µl aliquots.
mGFP-EB3 used for TIRF microscopy experiments was purified as previously described³¹. Briefly, mGFP-EB3 was expressed in E. coli BL-21 cells and purified by nickel-affinity chromatography, followed by size exclusion chromatography. Monomeric human EB3 calponin homology (CH) domain (residues 1-200) used for cryo-EM experiments was purified as previously described^{30 (link),32}. Briefly, EB3-CH was expressed in E. coli BL-21 cells and was purified by nickel-affinity chromatography, followed by size exclusion chromatography.

Estévez-Gallego J., Blum T.B., Ruhnow F., Gili M., Speroni S., García-Castellanos R., Steinmetz M.O, & Surrey T. (2025). Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap. Nature Communications, 16, 2396.

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Efficient scFv Expression and Purification

2025

For scFv expression, sequenced plasmids were used to transform chemically competent SHuffle T7 Express cells, after which a single colony was used to inoculate 5 mL LB supplemented with 100 μg/mL carbenicillin or ampicillin, and grown overnight at 37 °C. The next day, 5 mL fresh LB supplemented with 100 μg/mL carbenicillin or ampicillin was inoculated 1/100 with the overnight culture and cells were grown at 37 °C until reaching a density corresponding to an absorbance measured at 600 nm (Abs₆₀₀) ≈ 0.5–0.8. At this point, scFv expression was induced by addition of 0.1 mM IPTG, after which cells were incubated an additional 16 h at 30 °C. Cells were harvested by centrifugation (16,000 ×g, 4 °C) and resuspended in 1 mL BugBuster 10x Protein Extraction Reagent (Millipore). To prevent protein degradation, 10 μL of Halt Protease Inhibitor Cocktail (100x) (ThermFisher) was added. After incubation for 30 min, cell lysate was collected by centrifugation at 16,000 ×g for 20 min at 4 °C. Total protein in cell lysates was quantified by Bradford assay.
For scFv purification, cells were grown and induced identically as above, after which harvested cells were resuspended in PBS and lysed using an EmulsiFlex-C5 homogenizer (Avestin). The cell lysate was clarified by centrifugation at 15,000 ×g at 4 °C for 25 min and then mixed with HisPur Ni-NTA Resin (ThermoFisher). The resin-lysate mixture was incubated at room temperature with end-over-end mixing for 30 min. The mixture was then applied to a polypropylene gravity column and the lysate was allowed to completely pass through the column. The resin was then washed with 3x column volumes of wash buffer containing PBS supplemented with 25 mM imidazole and the protein was eluted with PBS supplemented with 250 mM imidazole. Purified fractions were applied to protein concentrators (10K MWCO; ThermoFisher) to change the buffer to PBS.

Wang W., Bunyatov M., Lopez-Barbosa N, & DeLisa M.P. (2025). Engineering affinity-matured variants of an anti-polysialic acid monoclonal antibody with superior cytotoxicity-mediating potency. bioRxiv.

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Recombinant Expression and Purification of Viral and Transcriptional Proteins

2025

hRSV NS1 (1-139), hMED25 ACID (389-543), hATF3 (1-181) or hATF3 bZIP (88-149) residues were subcloned into modified pET15b containing a tandem maltose binding protein (MBP) and His₆ tag as fusion partners and pACYC vectors (Novagen). hMED25 VWA was subcloned into a modified pGEX vector (GE Healthcare). All constructs, including mutants, were verified by Sanger sequencing. Plasmid vectors were transformed into Escherichia coli strain BL21(DE3) and grown in Luria-Bertani medium containing antibiotics at 37 °C to an optical density (A₆₀₀) of 0.6–0.7. Protein expression was induced with 0.5 mM isopropyl β-D-1-thiogalactopyranoside (IPTG) for 14 h at 18 °C. Cells were harvested by centrifugation at 30,000 × g and frozen in liquid nitrogen. Cells expressing NS1 or MED25 ACID were lysed using an Emulsiflex-C5 homogenizer (Avestin) and clarified by centrifugation at 69,673 × g. Proteins were purified using a series of affinity and ion exchange chromatographic columns followed by a Superdex 75 16/60 column (Cytiva) in buffer containing 20 mM Tris pH 8.0, 150 mM NaCl, and 2 mM tris(2-carboxyethyl) phosphine (TCEP). Recombinantly expressed MBP-ATF3 or ATF3 bZIP was either lysed in low salt conditions (MBP-ATF3_low/ATF3 bZIP_low; 25 mM phosphate buffer, pH 7, 150 mM NaCl, 20 mM imidazole, 5 mM bME) or high salt conditions (MBP-ATF3_high/ATF3 bZIP_high; 25 mM phosphate buffer, pH 7, 1 M NaCl, 20 mM imidazole, 5 mM bME) prior to purification on a Ni6 fast flow column (Cytiva). Purity of the protein was assessed by Coomassie blue staining of SDS-PAGE.

Kalita P., Khatavkar O., Uwase G., Korshunova Y., Hu Y., Wagner N.D., Xu J., Pan J., Nix J.C., Gross M.L., Brody S.L., Borek D., Amarasinghe G.K., Payton J.E, & Leung D.W. (2025). Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25. Nature Communications, 16, 2883.

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Purification and Labeling of Rv3718c Protein

2025

Hexahistidine-tagged Rv3718c was produced in Escherichia coli BL21(DE3) cells and grown in LB at 37°C. Expression was induced at OD₆₀₀ 0.6–0.7 with 0.1 mM isopropyl B-D-1-thiogalactopyranoside (IPTG) and grown for 4 hours at 37°C. Bacteria were pelleted and resuspended in buffer containing 50 mM NaH₂PO₄ pH 8.0, 100 mM NaCl, and 10 mM imidazole. All subsequent purification steps were performed at 4°C. Cells were lysed using the Emulsiflex-C5 homogenizer (Avestin, 2 cycles at 15,000 psi), and the homogenized lysate was centrifuged at 30,000 g for 1 hour. The clarified lysate was applied onto a column containing Ni Sepharose 6 resin (Cytiva Life Sciences) and washed with 20 column volumes of buffer containing 50 mM NaH₂PO₄ pH 8.0, 100 mM NaCl, and 20 mM imidazole. The protein was eluted with buffer containing 50 mM NaH₂PO₄ pH 8.0, 100 mM NaCl, and 250 mM imidazole. The eluent was concentrated using an Amicon Ultra 3 kD MWCO centrifugal filter and then exchanged into size-exclusion buffer (20 mM HEPES pH 8.0, 100 mM NaCl, 5% glycerol) using Zeba Spin Desalting Columns (MW cutoff 7 kD, 0.5 mL). Rv3718c was labeled with Alexa Fluor 647 NHS Ester (Invitrogen Catalog# A20106) for 30 minutes at room temperature in the dark. The sample was loaded onto a Superdex 75 Increase 10/300 Gl column (Cytiva Life Sciences) in size-exclusion buffer. Fractions were pooled, yielding protein concentrations of 8–14 µM, flash frozen in liquid nitrogen, and stored at −80°C.

Yoo J.H., Santarossa C., Thomas A., Ekiert D, & Darwin K.H. (2025). Characterization of a cytokinin-binding protein locus in Mycobacterium tuberculosis. Journal of Bacteriology, 207(3), e00003-25.

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Purification of Recombinant Human NuMA

2025

Recombinant human NuMA^{C-term S1} was purified from a pellet of 1 liter of Sf21 cell culture (≈11 g) resuspended in lysis buffer (50 mM KH₂PO₄, 50 mM Na₂HPO₄ [Thermo Fisher Scientific], 800 mM KCl, 2 mM MgCl_2, 1 mM EDTA, and 2 mM 2-ME, pH 8.0) supplemented with 50 U/ml Benzonase and protease inhibitors. Lysis was carried out using an Avestin EmulsiFlex-C5 homogenizer (two rounds). After clarification of the lysate by centrifugation (30,000 × g, 30 min, 4°C), the supernatant was filtered through a Millex-HV sterile syringe filter unit PVDF (0.45 μm; Merck) and loaded onto a 5 ml StrepTrap HP column. The column was washed with lysis buffer and eluted with Strep elution buffer (50 mM KH₂PO₄, 50 mM Na₂HPO₄, 500 mM KCl, 2 mM MgCl_2, 1 mM EDTA, 2 mM 2-ME, and 2.5 mM D-desthiobiotin, pH 8.0). The NuMA-containing fractions were pooled and concentrated (Amicon Ultra 4, 30 kDa MWCO). The Strep-tag II was cleaved off by incubating with TEV protease overnight at 4°C using a TEV-to-protein ratio of 1:30 (wt/wt). The cleaved protein was concentrated (Amicon Ultra 4, 30 kDa MWCO), ultracentrifuged (529,484 × g, 10 min, 4°C), and loaded on a HiLoad 16/600 Superdex 200 prep grade column. The elution was performed using size exclusion buffer (BRB80 [80 mM Pipes, 1 mM MgCl_2, 1 mM ethylene glycol bis(β aminoethyl ether) N,N,N′,N′ tetraacetic acid [EGTA]], 500 mM KCl, and 5 mM 2-ME, pH 6.8). The NuMA-containing peak fractions were pooled, exchanged into storage buffer (BRB80, 50 mM KCl, 5 mM 2-ME, pH 6.8), and concentrated (Amicon Ultra 4, 30 kDa MWCO) to ≈15 mg ml⁻¹. The yield was ≈1 mg protein/g pellet.

Colombo S., Michel C., Speroni S., Ruhnow F., Gili M., Brito C, & Surrey T. (2025). NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends. The Journal of Cell Biology, 224(4), e202408118.

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