Beckman avanti j e

Manufactured by Beckman Coulter

Sourced in United States

The Beckman Avanti J-E is a high-performance centrifuge designed for efficient and reliable separation of samples. It features a compact footprint and offers a wide range of speed and force options to meet the demands of various laboratory applications.

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Lab products found in correlation

Beckman ja 20 rotor, by Beckman Coulter (2 mentions) Valproic acid, by Merck Group (1 mentions) Caffeine, by Merck Group (1 mentions)

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Avanti J-E (58 citations)

6 protocols using beckman avanti j e

Efficient VLP Production in HEK293 Cells

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VLPs were expressed in HEK293 cells by transient transfection and concentrated by ultracentrifugation. Twenty-four hours prior to transfection cells were seeded at a density of 4×10⁵ cells ml⁻¹ in 175 cm² T flasks and incubated overnight (ON) at 37 °C and 5% CO₂. The transfection was performed using 5 μg of DNA per 10⁶ cells and PEI/DNA polyplexes were formed by adding PEI to plasmid DNA (in a 1.5:1 ratio) diluted in DMEM. Complexes were incubated for 15 min at room temperature (RT) and added to the culture. Four hours post-transfection (hpt), cell supernatant was removed and replaced by fresh complete medium containing valproic acid (1.68 mM) and caffeine (2.5 mM) (Sigma-Aldrich).
Seventy-two hpt cell supernatant containing VLPs was harvested and clarified by centrifugation at 4000 g for 20 min. The clarified supernatant was layered over a 30% sucrose cushion and centrifuged at 60,000 g for 5 h at 4 °C (Beckman JA-20 rotor, Beckman Avanti J-E, Beckman Coulter). VLP pellet was resuspended in PBS using 1% of the original volume and stored at 4 °C.

Garay E., Fontana D., Villarraza J., Fuselli A., Gugliotta A., Antuña S., Tardivo B., Rodríguez M.C., Gastaldi V., Battagliotti J.M., Alvarez D., Castro E., Cassataro J., Ceaglio N, & Prieto C. (2023). Design and characterization of chimeric Rabies-SARS-CoV-2 virus-like particles for vaccine purposes. Applied Microbiology and Biotechnology, 107(11), 3495-3508.

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Pseudotyped Lentivirus Production and Transduction

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An established protocol for pseudotyped lentivirus production was followed (Crawford et al. 2020 (link)). Briefly, HEK293T cells were co-transfected using PEI with the plasmids HDM-Hgpm2, HDM-tat1b, pRC-CMV-Rev1b, and pHAGE2-CMV-ZsGreen-W, and a plasmid encoding the envelope protein, i.e., HDM-IDTSpike-fix, for wt S protein or pLV-S-RVG for the fusion protein pseudotype. As a negative control, a lentiviral stock without any envelope protein was constructed. Forty-eight hours post transfection, supernatants were collected and clarified at 4000 g for 20 min, and then concentrated by ultracentrifugation at 60,000 g for 5 h at 4 °C (Beckman JA-20 rotor, Beckman Avanti J-E, Beckman Coulter). Pellets were resuspended in DMEM with 3% of the original volume and stored at −70 °C.
HEK293 cells expressing ACE2 were used to analyze S-RVG ability to interact with ACE2 receptor and mediate lentiviral transduction. For this, HEK293-ACE2 or wt HEK293 cells were plated on 96-well plates at 3.5×10⁴ cells ml⁻¹ 24 h prior to the transduction experiment. Then, culture supernatants were removed and concentrated lentivirus samples diluted 1:2 in DMEM complete medium were added over the cells by triplicate. Seventy-two hours later, ZsGreen expression on transduced cells was measured by flow cytometry with a GUAVA EasyCyte cytometer using Guava Express Plus Software.

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Actomyosin Surface Hydrophobicity Analysis

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The surface hydrophobicity of actomyosin was examined according to the method of Zhao et al [14 ] with slight modifications. Each actomyosin was diluted to 2.0 mg/mL using 0.6 M KCl buffer. Each actomyosin solution (2 mL) was placed in a 7-mL centrifuge tube and heated in a water bath (Julabo TW20, Germany) from 20°C to 85°C at 1°C/min. Twenty-one tubes were placed in water bath (Julabo TW20, Germany) for each actomyosin. Three tubes were taken out every 10°C intervals (total seven sampling points for each actomyosin), and then transformed in an ice water bath for 10 min. Each actomyosin suspension (2 mL) was mixed with 80 μL of bromophenol blue (1 mg/mL) (BPB). The KCl buffer (0.6 M KCl, 20 mM K₂HPO₄/KH₂PO₄, pH 7.0, 2 mL) with 80 μL of BPB addition was used as the control. The control and samples were placed at 20°C, mixed for 10 min and centrifuged at 4,000 g for 15 min (Beckman Avanti J-E, Beckman Coulter, USA). After centrifugation, the liquid supernatant was diluted 10 times. The absorbance of the control (A₀) and the sample (A_s) were determined at 595 nm. The 0.6 M KCl buffer was used as reference. The BPB bond content was expressed as the following equation: BPB bound (μg) = 80 μg×(A₀–A_s)/A_o.

Li K., Liu J.Y., Fu L., Zhao Y.Y, & Bai Y.H. (2018). Comparative study of thermal gelation properties and molecular forces of actomyosin extracted from normal and pale, soft and exudative-like chicken breast meat. Asian-Australasian Journal of Animal Sciences, 32(5), 721-733.

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Evaluating Meat Protein Water Binding

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The WBC of gels has an impact on several quality traits and represents the ability of proteins to bind to and retain water. This property is also largely used to evaluate the quality and yield of meat products.
A frozen sample (about 2 g) w_s was placed in a 7 mL centrifuge tube w_t, then centrifuged in a Beckman Avanti J-E centrifuge (Beckman Coulter, Fullerton, CA, USA). All samples were centrifuged for 10 min at 10,000× g at 4 °C. After centrifuging, the water was drawn off with filter paper. Then gels were weighed w_g. WBC was expressed as percent water retained per 100 g water present in the sample prior to centrifuging. Treatments were performed in triplicate and measurements were carried out in triplicate, in order to understand the stability of gels. WBC was measured by a modification of a published method [26 (link)]. WBC = (w_g − w_t/w_s − w_t) × 100%.

Cao Y., Zhao L, & Li H. (2023). Effects of Combining High Pressure Processing Treatments and Konjac Glucomannan and Sodium Caseinate on Gel Properties of Myosin Protein. Foods, 12(4), 691.

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Muscle Protein Isolation from Meat Samples

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MPs were prepared from meat samples after the tumbling process following the method of Han et al. [15] . Briefly, the meat samples were homogenized at 10,000 rpm with 4 volumes (w/v) of precooled buffer A (0.1 M KCl, 1 mM EGTA, 20 mM K₂HPO_4, 2 mM MgCl₂, 20 mM KH₂PO₄, pH 7.0). The mixture was centrifuged at 2,000 × g and 4 °C for 15 min (Beckman Avanti J-E, Beckman Coulter, Fullerton, CA, USA). After pouring the supernatant, the procedures were repeated twice using buffer A. Then, the precipitate was clarified twice with 4 volumes (w/v) of buffer B (0.1 M NaCl). The clean precipitates were filtered with single gauze to discard connective tissues before the last time of centrifugation, and the pellets were collected. All the above processes were kept in an ice box. Finally, MPs pellets were dissolved in buffer C (0.6 M NaCl, 20 mM K₂HPO_4, 20 mM KH₂PO₄, pH 7.0) for further analysis. The protein concentration was measured by the Biuret method [16] (link).

Zhang R., Xing L., Kang D., Zhou L., Wang L, & Zhang W. (2021). Effects of ultrasound-assisted vacuum tumbling on the oxidation and physicochemical properties of pork myofibrillar proteins. Ultrasonics Sonochemistry, 74, 105582.

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Protein Determination by Biuret Method

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The methods of protein determination were followed by McDonnell et al. [22] (link) with a slight change. After tumbling, the brine was collected and centrifuged at 10,000×g for 10 min at 4 °C to precipitate meat crumbs (Beckman Avanti J-E, Beckman Coulter, Fullerton, CA, USA). The protein content of the supernatant was measured by the Biuret method with the BSA as the standard protein [23] (link).

Zhang R., Zhang J., Zhou L., Wang L, & Zhang W. (2021). Influence of ultrasound-assisted tumbling on NaCl transport and the quality of pork. Ultrasonics Sonochemistry, 79, 105759.

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