Fa 45 24 11 rotor

Manufactured by Eppendorf

Sourced in Germany

The FA-45-24-11 rotor is a high-speed centrifuge rotor designed for use with Eppendorf's centrifuge models. It has a maximum capacity of 24 x 11 mL tubes and can reach a maximum speed of 18,000 rpm, generating a maximum relative centrifugal force (RCF) of 45,000 x g. The rotor is suitable for a variety of common laboratory applications that require high-speed centrifugation.

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Lab products found in correlation

Centrifuge 5424r, by Eppendorf (3 mentions) Chlorpropamide, by Thermo Fisher Scientific (1 mentions) Centrifuge 5417r, by Eppendorf (1 mentions) Prominence hplc system, by Shimadzu (1 mentions) Human serum h4522, by Merck Group (1 mentions) C18 analytical column, by Waters Corporation (1 mentions)

6 protocols using fa 45 24 11 rotor

In vivo BBB Permeability Assay

Cited 2 times

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BBB permeability was examined using in vivo permeability assay as described previously [40 (link), 41 (link)]. Briefly, sterile Evans blue solution (2% in saline, 80 μl) and FITC-Dextran (4 kD, 25 mg/ml, 50 μl) were injected intravenously into control and PKO mice. After 6 h, these mice were transcardially perfused with 50 ml saline. The brains were then collected and cut into left and right hemispheres. Each hemisphere was carefully weighed and homogenized in 800 μl PBS and centrifuged at 16,363 g (Eppendorf FA-45-24-11 rotor) for 20 min at 4 °C. For Evans blue, the supernatant was collected and read in a spectrophotometer (Molecular devices-SpectraMax, California, USA) at 620 nm. For FITC-Dextran, the supernatant was collected and read in a fluorescent plate reader (Molecular devices-SpectraMax, California, USA) at 485/528 nm. Each sample was measured in triplicates, and the average of these technical replicates was used as one biological replicate.

Gautam J., Xu L., Nirwane A., Nguyen B, & Yao Y. (2020). Loss of mural cell-derived laminin aggravates hemorrhagic brain injury. Journal of Neuroinflammation, 17, 103.

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Mass Spectrometry Analysis of Metabolites

Cited 1 time

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Samples were thawed on ice and resuspended in ice-cold high-performance LC–grade water spiked with 1 μM chlorpropamide (Alfa Aesar) to a concentration of 1 × 10⁶ cells/μl before loading on a Thermo Exactive Plus orbitrap liquid chromatography coupled mass spectrometer. Samples were vortexed and centrifuged (Eppendorf Centrifuge 5424R and FA-45–24-11 Rotor) for 10 min at 4°C at 15,000 rpm. The supernatant was then added to 800-μl CRIMP vials (Thermo Fisher Scientific) for mass spectrometry loading. As an additional quality control, pooled samples were constituted with 5 to 10 μl from each sample and run in triplicate on the mass spectrometer. Molecules in samples were separated using an XSelect HSS T3 2.5 μm C18 Waters column with a 25-min gradient of 3% aqueous methanol, 15 mM acetic acid, and 10 mM tributylamine as the ion pairing agent in negative ionization mode (negative electrospray ionization) and detected using the Thermo Exactive Plus orbitrap (58 (link)).

Arendse L.B., Murithi J.M., Qahash T., Pasaje C.F., Godoy L.C., Dey S., Gibhard L., Ghidelli-Disse S., Drewes G., Bantscheff M., Lafuente-Monasterio M.J., Fienberg S., Wambua L., Gachuhi S., Coertzen D., van der Watt M., Reader J., Aswat A.S., Erlank E., Venter N., Mittal N., Luth M.R., Ottilie S., Winzeler E.A., Koekemoer L.L., Birkholtz L.M., Niles J.C., Llinás M., Fidock D.A, & Chibale K. (2022). The anticancer human mTOR inhibitor sapanisertib potently inhibits multiple Plasmodium kinases and life cycle stages. Science translational medicine, 14(667), eabo7219.

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Quantification of Peptide Concentration

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Samples containing 180 µM insulin or PTH(1-34) and 720 µM penetratin were subjected to ultracentrifugation (25,000× g, 30 min, 20 °C) using a 5417 R centrifuge equipped with a FA-45-24-11 rotor (Eppendorf, Hamburg, Germany). Insulin, PTH(1-34), and penetratin left in the supernatant was quantified by reverse phase high-pressure liquid chromatography (HPLC) using a Prominence HPLC system (Shimadzu, Kyoto, Japan) equipped with an Aeris PEPTIDE XB-C18 column (3.6 µm core shell particles; Torrance, CA, USA). A gradient elution from 20–70% mobile phase B (acetonitrile/ultrapure water 95:5 and 0.1% trifluoroacetic acid (TFA) (v/v)) in mobile phase A (ultrapure water/acetonitrile 95:5 and 0.1% TFA (v/v)) over 10 min was applied using a flow rate of 0.8 mL/min and an injection volume of 10 µL. UV-detection was performed at 218 nm.

Kristensen M., Guldsmed Diedrichsen R., Vetri V., Foderà V, & Mørck Nielsen H. (2020). Increased Carrier Peptide Stability through pH Adjustment Improves Insulin and PTH(1-34) Delivery In Vitro and In Vivo Rather than by Enforced Carrier Peptide-Cargo Complexation. Pharmaceutics, 12(10), 993.

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Rumen In Vitro Fermentation Assay

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After flushing
with nitrogen once again, the tubes were sealed with rubber stoppers
and aluminum crimp caps. The tubes were incubated for various time
periods (0, 0.5, 1, 2, 4, 6, and 20 h) at 39 °C while being shaken
at 250 rpm (simulation of 1–2 rumen contraction per minute).
The incubation was stopped by adding 14 mL of 0.05 M H₂SO₄. Samples were centrifuged at 363 g for 15 min (Thermo
Fisher Scientific Multifuge X1R Pro with a TX-400 rotor, Waltham,
USA), and 500 μL of the supernatant was filtered through a centrifugal
filter (modified Nylon 0.2 μm, VWR, Radnor, USA) at 23,500 g
for 10 min (Eppendorf 5424 R centrifuge with an FA-45-24-11 rotor,
Hamburg, Germany). Samples were stored at 5 °C until mass spectrometric
analysis. The storage period was not more than 14 days. The redox
potential and the pH were measured before incubation and after each
sampling to ensure rumen physiological conditions. Gas pressure was
measured hourly with a gas transducer to confirm fermentation (GMH
3161-07-EX, GHM Messtechnik GmbH, Regenstauf, Germany). Gas production
was calculated according to Mauricio et al. To distinguish between
nonenzymatic and enzymatic reactions, controls were included in each
run.^{29 (link)} The control approach was performed
in the same way as the incubated samples, but the ruminal inoculum
had been autoclaved at 121 °C for 3 h prior to incubation.

Taenzer J., Gehling M., Klevenhusen F., Saltzmann J., Dänicke S, & These A. (2022). Rumen Metabolism of Senecio Pyrrolizidine Alkaloids May Explain Why Cattle Tolerate Higher Doses Than Monogastric Species. Journal of Agricultural and Food Chemistry, 70(33), 10111-10120.

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Serum-Mediated Peptide Degradation Kinetics

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Diluted human serum (25%; H4522 human serum, Sigma) was incubated at 37 °C for 15 min and added to peptide stock in DMSO to ~100 μM final peptide concentration. The solution was incubated at 37 °C and 50-μL aliquots were withdrawn at various time points. This solution was mixed with 50 μL of 15% trichloroacetic acid (TCA) in MeOH and 50 μL of acetonitrile, and the mixture was stored at 4 °C overnight. Finally, the samples were centrifuged at 15,000 rpm for 10 min in a microcentrifuge equipped with Eppendorf FA-45-24-11 rotor, and the supernatant was analyzed by reversed-phase HPLC equipped with an analytical C18 column (Waters). The amount of peptide remaining at each time point was determined by integrating the area under the peptide peak in the resulting HPLC chromatogram (monitored at 214 nm) and comparing to the peptide amount at time zero.

Buyanova M., Cai S., Cooper J., Rhodes C., Salim H., Sahni A., Upadhyaya P., Yang R., Sarkar A., Li N., Wang Q.E, & Pei D. (2021). Discovery of a Bicyclic Peptidyl Pan-Ras Inhibitor. Journal of medicinal chemistry, 64(17), 13038-13053.

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Centrifugation of Diluted Dispersions

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Slightly modifying sample preparation methods from previous studies (Hansen et al. 2021a (link)), 1.25 g aliquots of 5-times diluted dispersions were pipetted into tubes (1.5 mL graduated tubes with flat caps, Fisherbrand®, Fisher Scientific, Hampton, NH, USA) and centrifuged at 12,000 rpm (~13,523 x g) and 20 °C for 20 min in a microcentrifuge (Centrifuge 5424 R with FA-45-24-11 rotor, Eppendorf, Hamburg, Germany). Tubes were observed after centrifugation.

Hansen M.M., Hartel R.W., & Roos Y.H. (2021). Effects of Aronia polyphenols on the physico-chemical properties of whey, soy, and pea protein isolate dispersions. Food Production Processing and Nutrition, 3(1).

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