F4503

Manufactured by Merck Group

Sourced in China

F4503 is a laboratory equipment product manufactured by Merck Group. It is designed for general laboratory use. The core function of F4503 is to provide a reliable and consistent platform for various laboratory tasks and experiments. Further details on the specific intended use or applications of this product are not available.

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Lab products found in correlation

C2506, by Merck Group (1 mentions) V2876, by Merck Group (1 mentions) C3934, by Merck Group (1 mentions) Superdex 200 increase 10 300 gl column, by Cytiva (1 mentions) Ferrozine, by Merck Group (1 mentions) Histopaque 1077, by Merck Group (1 mentions) L4391, by Merck Group (1 mentions) Histopaque 1119, by Merck Group (1 mentions) P1585, by Merck Group (1 mentions)

5 protocols using f4503

Neutrophil Isolation and Stimulation Protocol

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Neutrophils were isolated using the Human and Mouse Neutrophil Isolation and Purification Kit (TBD Sciences, Tianjin, China) for subsequent experiments. Briefly, neutrophils were isolated from human or mouse blood samples by stratification using the Neutrophil Isolation Reagent and centrifuged at 800 g for 30 min at room temperature. The lower band containing neutrophils was carefully aspirated and washed with PBS after removing erythrocytes with erythrocyte lysate. The remaining cells were resuspended with 1640 (Gibco, US) containing 10% fetal bovine serum (FBS) (Gibco). The isolated neutrophils were then inoculated in 6-well plates (2 × 10⁶ cells per well). Neutrophils were stimulated in vitro with 50 nM PMA (MKBio, Shanghai, China) or ferritin (10–1000 nM, F4503, Sigma-Aldrich) for 4 hours.

Zhang H., Wu D., Wang Y., Shi Y., Shao Y., Zeng F., Spencer C.B., Ortoga L., Wu D, & Miao C. (2024). Ferritin-mediated neutrophil extracellular traps formation and cytokine storm via macrophage scavenger receptor in sepsis-associated lung injury. Cell Communication and Signaling : CCS, 22, 97.

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Gel Filtration Chromatography for Peanut Protein Analysis

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PPE (1 mg/mL), Ara h 1 (1 mg/mL), Ara h 2 (0.5 mg/mL), Ara h 3 (0.5 mg/mL) and Ara h 6 (0.5 mg/mL) in PBS were filtered through a 0.2 µm filter and individually loaded (50 µL) onto a Superdex 200 Increase 10/300 GL column (Cytiva, Uppsala, Sweden) connected to an ÄKTA pure 25 M system (Cytiva). Each protein sample was eluted at RT with PBS at an elution rate of 0.4 mL/min. The eluted proteins were detected by absorbance at 215 and 280 nm. The column was calibrated for molecular weight (MW) determination by applying a standard mixture consisting of 0.3 mg/mL ferritin (440 kDa; F4503, Sigma-Aldrich), 1 mg/mL conalbumin (79 kDa; C0880, Sigma-Aldrich), 1 mg/mL carbonic anhydrase (29 kDa; C3934, Sigma-Aldrich), 1 mg/mL cytochrome C (14 kDa; C2506, Sigma-Aldrich), 0.5 mg/mL vitamin B12 (1.3 kDa, V2876, Sigma-Aldrich). The presence and approximate quantification of Ara h 1, Ara h 2, Ara h 3 and Ara h 6 present in PPE was determined by overlapping peaks between PPE and the individual allergen followed by calculating area under the curve (AUC).

Sztuk T.K., Rigby N.M., Nørskov-Nielsen L., Koppelman S.J., Sancho A.I., Knudsen N.P., Marsh J., Johnson P., Gupta S., Mackie A.R., Larsen J.M, & Bøgh K.L. (2023). Dose and route of administration determine the efficacy of prophylactic immunotherapy for peanut allergy in a Brown Norway rat model. Frontiers in Immunology, 14, 1121497.

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Monitoring Ferrous Iron in Ferritin

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Fe²⁺ levels of a solution of horse spleen ferritin (SIGMA-Aldrich, F4503) were monitored by absorption spectrophotometry of the Fe²⁺-ferrozine complex. All solutions were freshly prepared with the assay buffer (5M ammonium acetate, pH 7). Ferritin was prepared at 3 mg/mL, ferrozine (SIGMA-Aldrich, 160601) was prepared at 4 mM, and L-Ascorbic acid was prepared at 1M. Ferritin samples (100 μL) were transferred to a 96 well plate. To measure ferrous iron (Fe²⁺), 5 μL of assay buffer was added to each sample. To measure total iron (Fe²⁺ plus Fe³⁺), 5 μL of 1M of L-Ascorbic acid was added to each sample. L-Ascorbic acids acts as the reducing agent, allowing the measurement of total iron. Samples were mixed and incubated for 30 min at room temperature. Next, 100 μL of 4 mM ferrozine was added to each sample. Samples were mixed and incubated for 1-h protected from light. Absorbance was measured at 550 nm with a plate reader (EnVision Plate reader 21049). The RF and No RF ferritin samples were processed simultaneously. For RF groups, RF was applied at 12 μT with the 25-cm RF coil during the entire period of the experiment (1.5-h). For No RF groups, samples were maintained in the same room, but placed where RF was negligible. The calibration curve was obtained with Fe²⁺ standards from 0 to 50 μM, freshly prepared every time the assay was conducted.

Hernández-Morales M., Shang T., Chen J., Han V, & Liu C. (2020). Lipid Oxidation Induced by RF Waves and Mediated by Ferritin Iron Causes Activation of Ferritin-Tagged Ion Channels. Cell reports, 30(10), 3250-3260.e7.

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Isolating and Stimulating Mouse Neutrophils

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BMDNs were isolated by density gradient centrifugation using Histopaque 1119 (11191, Sigma-Aldrich) and Histopaque 1077 (10771, Sigma-Aldrich). Total bone marrow cells were collected from tibias and femurs and the RBCs were lysed. Mature neutrophils were purified by centrifugation for 30 min at 845 × g without braking on a Histopaque 1119 and Histopaque 1077. The neutrophils were collected at the interface of the Histopaque 1119 and Histopaque 1077. Mice neutrophils (1 × 10⁶ cells/mL) cultured in RPMI 1640 supplemented with 10% FBS and were stimulated with ferritin (100 nM, F4503, Sigma-Aldrich), LPS (100 ng/mL, L4391, Sigma-Aldrich) or PMA (20 nM, P1585, Sigma-Aldrich) for 3.5 h at 37 °C.

Jia J., Wang M., Meng J., Ma Y., Wang Y., Miao N., Teng J., Zhu D., Shi H., Sun Y., Liu H., Cheng X., Su Y., Ye J., Chi H., Liu T., Zhou Z., Wan L., Chen X., Wang F., Zhang H., Ben J., Wang J., Yang C, & Hu Q. (2022). Ferritin triggers neutrophil extracellular trap-mediated cytokine storm through Msr1 contributing to adult-onset Still’s disease pathogenesis. Nature Communications, 13, 6804.

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Mitochondrial Protein Complexes Analysis

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Starting material was two 150 mm dishes with cells at 80–90% confluency for each condition. The cells were released with trypsin and the pellet washed with PBS. Crude mitochondria were enriched according to Wieckowski et al. (2009) (link). Briefly, cells were homogenized in isolation buffer (225 mM mannitol, 75 mM sucrose, 0.1 mM EGTA, and 30 mM Tris-HCl, pH 7.4) with 20 strokes in a Potter-Elvehjem homogenizer at 6000 rpm, 4°C. Unbroken cells and nuclei were collected by centrifugation at 600 × g for 5 min and mitochondria recovered from this supernatant by centrifugation at 7000 × g for 10 min. After one wash of this pellet, membranes were solubilized in 1.5 M aminocaproic acid, 50 mM Bis-Tris, pH 7.0, buffer with antiproteases and 4 g/g (detergent/protein) digitonin. Proteins were separated by blue native electrophoresis in 3–12% gradient gels (Diaz et al., 2009 ; Timon-Gomez et al., 2020 (link)) using 10 mg/ml ferritin (404 and 880 kDa, Sigma F4503) and BSA (66 and 132 kDa) as molecular weight standards.

Werner E., Gokhale A., Ackert M., Xu C., Wen Z., Roberts A.M., Roberts B.R., Vrailas-Mortimer A., Crocker A, & Faundez V. (2022). The mitochondrial RNA granule modulates manganese-dependent cell toxicity. Molecular Biology of the Cell, 33(12), ar108.

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