Ferritin

Manufactured by Merck Group

Sourced in United States, Germany

Ferritin is a lab equipment product that is used to measure the amount of ferritin, a protein that stores iron, in the body. It provides a quantitative assessment of the body's iron stores.

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Lab products found in correlation

Bovine serum albumin (bsa), by Merck Group (9 mentions) Thyroglobulin, by Merck Group (7 mentions) Ovalbumin (ova), by Merck Group (6 mentions) Cytochrome c, by Merck Group (5 mentions) Aldolase, by Merck Group (4 mentions) Alcohol dehydrogenase, by Merck Group (3 mentions) Apoferritin, by Merck Group (3 mentions) Transferrin, by Merck Group (2 mentions) Sephacryl s 300 hr, by Merck Group (2 mentions) Aprotinin, by Merck Group (2 mentions) Scopoletin, by Merck Group (2 mentions) Neuronal nuclei (neun), by Merck Group (2 mentions) Sodium chloride (nacl), by Merck Group (2 mentions) Ethylene diamine tetraacetic acid (edta), by Merck Group (2 mentions) β actin, by Merck Group (2 mentions) Ecl kit, by Thermo Fisher Scientific (2 mentions) Ampicillin, by GoldBio (1 mentions) Arabinose, by GoldBio (1 mentions) Ebastine, by Cayman Chemical (1 mentions) Isopropyl β d 1 thiogalactopyranoside (iptg), by GoldBio (1 mentions)

Close spelling variants of this product

Ferritin from equine spleen (11 citations) Horse spleen ferritin (11 citations) Human Ferritin ELISA Kit (4 citations) Holo-ferritin (4 citations) Anti-ferritin (3 citations) Anti-horse spleen ferritin antibody (3 citations) Ferritin from horse spleen (3 citations) Rabbit anti-human Ferritin (2 citations) Rabbit anti-ferritin antibody (2 citations) Anti‐L‐Ferritin (2 citations)

41 protocols using ferritin

Ferritin Iron Mobilization Kinetics

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Ferritin (horse spleen) and NADPH-P 450 reductase (rabbit liver) were obtained from Sigma-Aldrich Co. (St. Louis, MO).
The standard reaction mixture for iron mobilization from Ferritin contains 1.9 μM Ferritin, 1U NADPH-P 450 reductase, 20 μM bathophenanthroline disulfonic acid 2Na salt in 20 mM phosphate buffer, pH 7.4. bathophenanthroline is used as a quantity regent of iron by binding to ferrous iron and forming orange-red chelate. We measured the quantity of released ferrous iron in real time using the spectrophotometer (U-3900, Hitachi High-Tsch Science Corporation, Japan) after adding 100 μM NADPH to the standard reaction mixture. The quantity of released ferrous iron was calculated from absorbance at 530 nm by using a molar absorbance coefficient of 22.1 × 10 3 M -1 cm -1 for bathophenanthroline.
To investigate the effect of superoxide dismutase on the reductive mobilization of iron, 10 μM superoxide dismutase added to the standard reaction mixture. In another experiment to elucidate the mechanism of Ferritin iron reduction, 2 mM ferricyanide or 6.7 μM cytochrome C was added each to the standard reaction mixture.
No less than 4 experiments were performed separately. The results are expressed as the representative data for all the experiments.

Takaishi K, & Kitahata H. (2019). Electrons released from both flavins of NADPH-P450 reductase contribute to the reductive mobilization of iron from ferritin. The journal of medical investigation : JMI, 66(3.4).

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Controlled Growth of Random SWNTs

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The random SWNT networks used here are grown using thermal chemical vapor deposition on quartz substrates. The process flow is as follows: (1) A quartz substrate is cleaned by ultrasonication in acetone and IPA to remove organic contaminants and then dipped into a piranha solution (a 3:1 volumetric mixture of concentrated sulphuric acid to 30 hydrogen peroxide solution) for 30 min to make the quartz surface extremely hydrophilic; (2) The catalyst solution of ferritin (Aldrich; diluted with de-ionized water at a volumetric ratio of 1:80) is spin-coated on the quartz substrate; (3) The quartz substrate is heated to 800 °C in a quartz tube to oxidize ferritin into iron oxide nanoparticles; (4) The quartz tube is then further heated to 925 °C in 100 s.c.c.m. hydrogen gas flow for 10 min to reduce the iron oxide to iron; (5) 30 s.c.c.m. argon gas and 15 s.c.c.m. hydrogen gas flow through an ethanol (carbon source) bubbler into the quartz tube while maintaining temperature (925 °C) for 15 min. The density of the random SWNTs is controllable through control of the concentration of ferritin solution and carrier gases (H₂ and Ar) flow rates.

Zou J., Zhang K., Li J., Zhao Y., Wang Y., Pillai S.K., Volkan Demir H., Sun X., Chan-Park M.B, & Zhang Q. (2015). Carbon Nanotube Driver Circuit for 6 × 6 Organic Light Emitting Diode Display. Scientific Reports, 5, 11755.

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Mycobacterial Growth Assays with Ferritin

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H37Rv and the ΔbfrAB mutant were grown in 7H9 complete medium until log phase. Then the cultures were spun down and were washed twice in 7H9 medium only. The pellet was resuspended in 7H9 medium only and was inoculated into different media at an optical density (OD) of 0.05. Cultures were grown in triplicate in a 96-well plate, and the absorbance at 600 nm was taken on a daily basis. The composition of different carbon source media was as follows: 7H9 medium, 0.5% fatty-acid-free BSA (catalog no. A7030; Sigma), 0.085% sodium chloride (Sigma), and 0.025% tyloxapol (Sigma), with sole carbon sources or a mixture of 0.2% glucose (HiMedia), 0.5% glycerol (HiMedia), and oleic acid (0.09 mM, 0.18 mM, or 0.36 mM; Sigma).
For the growth assay in the presence or absence of ferritin (catalog no. F4503; Sigma), different concentrations of ferritin (1 ng, 100 ng, 1 μg/ml, 100 μg/ml) were added to a medium with glycerol as the sole carbon source. Apoferritin (catalog no. A3660; Sigma) was inactivated by heating at 95°C for 5 min. Apoferritin and heat-inactivated apoferritin were added at different concentrations (1 ng, 100 ng, 1 μg/ml, 100 μg/ml) to a medium with glycerol as the sole carbon source.

Nandy A., Mondal A.K., Pandey R., Arumugam P., Dawa S., Jaisinghani N., Rao V., Dash D, & Gandotra S. (2018). Adipocyte Model of Mycobacterium tuberculosis Infection Reveals Differential Availability of Iron to Bacilli in the Lipid-Rich Caseous Environment. Infection and Immunity, 86(6), e00041-18.

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Graphene-Based Biosensing Platform Fabrication

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Graphene on 25-µm-thick copper foil (Gr/Cu) synthesized through chemical vapor deposition (CVD) was purchased from Chongqing Graphene Technology Co., Ltd. (also known as Chongqing Moxi Technology). The following materials were ordered from Millipore Sigma (formerly Sigma-Aldrich): ferritin, anti-ferritin antibody, dimethylformamide (DMF), Tween-20, ethanolamine (ETA), and ~150 mM phosphate-buffered saline (1× PBS, pH 7.4 at 25 °C). Here, 1.5 mM PBS (0.01× PBS) was prepared by diluting 1× PBS appropriately with de-ionized water. Furthermore,1-pyrenebutanoic acid, succinimidyl ester (PASE) was purchased from Thermofisher Scientific.

Oshin O., Kireev D., Hlukhova H., Idachaba F., Akinwande D, & Atayero A. (2020). Graphene-Based Biosensor for Early Detection of Iron Deficiency. Sensors (Basel, Switzerland), 20(13), 3688.

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Membrane Protein Reconstitution Protocol

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Ampicillin, arabinose, chloroamphenicol and IPTG were from Gold Biotechnology. NADPH and NADP were obtained from P212121.com. Protein standards—thyroglobulin, ferritin, bovine serum albumin, and cytochrome c, were purchased from Sigma. Phospholipids 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L serine (POPS) were purchased from Avanti Polar Lipids. The phospholipid 1-hexadecanoyl-2-(1-pyrenedecanoyl)-sn-glycero-3-phosphocholine (PYRPC) was obtained from Life Technologies. Amberlite XAD 2 was procured from Supelco. Nanosep MF (0.2 μM) and Amicon Ultra (10,000 MWCO) centrifugal filters were bought from Millipore. AA and ebastine were purchased from Cayman Chemical. All other materials and reagents used were purchased from Sigma-Aldrich and Fisher Scientific.

McDougle D.R., Baylon J.L., Meling D.D., Kambalyal A., Grinkova Y.V., Hammernik J., Tajkhorshid E, & Das A. (2015). Incorporation of Charged Residues in the CYP2J2 F-G Loop Disrupts CYP2J2-Lipid Bilayer Interactions. Biochimica et biophysica acta, 1848(10 0 0), 2460-2470.

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Protein-Iron Complex Characterization

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Standard buffer consisted of 25 mM sodium bicarbonate (Fisher), 20 mM Tris-base (Fisher), and 10 mM NaCl (EMD), prepared in high purity water and adjusted to pH 7.4 using trace-grade HCl (Fisher). Stock solutions of transferrin (Athens Research and Technology) (76 μM) and bovine serum albumin (Sigma) (1.2 mM) were prepared in the standard buffer. A stock solution of Fe^III citrate (70 μM) was prepared by mixing 40 mM ferrous ammonium sulfate (Fisher) with 120 mM sodium citrate (Fisher), and adjusting the pH to 5 using citric acid (Acros Organics) (final concentrations obtained using deionized water). Iron solutions were mixed with select protein samples, transferrin:iron at molar ratio 1:1 and albumin:iron at molar ratio 0.058:1. Protein and iron solutions were mixed, incubated for 1 hr, then passed through a 0.2 μm filter (VWR). transferrin ± Fe and albumin ± Fe solutions were mixed 1:1 with each other or diluted 1:1 with standard buffer. A solution of alcohol dehydrogenase (Sigma) was prepared (10 mg/mL) in standard buffer, and mixed 1:1:1 with Fe^III transferrin (prepare 1:1 Fe^III citrate) and albumin solutions (in this sample, only transferrin had Fe^III citrate). Ferritin (Sigma; 2 mg/mL) was prepared in standard buffer except lacking bicarbonate. These solutions were then passed though the Superdex 200 GL column as described above.

Dziuba N., Hardy J, & Lindahl P.A. (2019). Low-molecular-mass iron complexes in blood plasma of iron-deficient pigs do not originate directly from nutrient iron. Metallomics : integrated biometal science, 11(11), 1900-1911.

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Immunohistochemical Analysis of Putamen

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Deparaffinized 6-μm sections of the putamen were incubated with 3% H₂O₂ in methanol for 20 min to block endogenous peroxidase activity. Sections were microwaved in trisodium citrate solution (pH 6.5) for antigen retrieval and blocked with 1.5% normal sera for 30 min before incubation with the primary antibody for 1h at room temperature [glial fibrillary acidic protein: GFAP (1:500, Dako, Ely, UK); CD68 (1:100, Dako); CD163 (1:100, Serotec, Kidlington, UK); fibrinogen (1:400, Alere Ltd, Stockport, UK); ferritin (1:1000, Sigma, Poole, UK)]. The avidin-biotin horseradish peroxidase (ABC-HRP) complex method was used (Vectastain Elite kit, Vector Laboratories, Peterborough, UK), with diaminobenzidine (DAB) as the substrate. Five random regions within the area of interest were selected (×20 magnification; Cell∧R, Olympus, Southend-on-Sea, UK), and the percentage area immunoreactivity of the image analysed using analysis^∧D software (Olympus Biosystems, Planegg, Germany) following delineation and exclusion of vascular profiles and voids in the sections.

Janaway B.M., Simpson J.E., Hoggard N., Highley J.R., Forster G., Drew D., Gebril O.H., Matthews F.E., Brayne C., Wharton S.B, & Ince P.G. (2014). Brain haemosiderin in older people: pathological evidence for an ischaemic origin of magnetic resonance imaging (MRI) microbleeds. Neuropathology and Applied Neurobiology, 40(3), 258-269.

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Protein Size Estimation by Superose 6 Chromatography

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A Superose® 6 Increase 3.2/300 column (Sigma-Aldrich Chemie GmbH, Taufkirchen, Germany), equilibrated with reaction buffer, was loaded with 30 µl of a 10 µM protein solution. Proteins were eluted using an ÄKTA purifier 10 system (GE Healthcare, Munich, Germany) at 7 °C and a flow rate of 0.03 ml/min. The standard proteins thyroglobulin (669 kDa) Ferritin (440 kDa), Aldolase (158 kDa), Conalbumin (75 kDa) and Ovalbumin (44 kDa) (Sigma-Aldrich Chemie GmbH, Taufkirchen, Germany) were used for protein mass estimation. Chromatograms were recorded using the software UNICORN (version 5.10).

Gewehr L., Junglas B., Jilly R., Franz J., Zhu W.E., Weidner T., Bonn M., Sachse C, & Schneider D. (2023). SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features. Nature Communications, 14, 2156.

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Carbon Nanotube Growth via Ferritin Catalysis

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Ferritin (Sigma Aldrich, F4503) was used as a catalyst for carbon nanotube growth in this study. Ferritin was mixed with DI water in a 10:1 ratio, and this fluid was dripped onto the scratched substrate. After a 15 minute incubation period, the residual solution was blown away using a nitrogen air gun. The substrate was then placed in a 1 inch atomic pressure chemical deposition (APCVD) furnace and heated to 900°C under an Ar environment. A CH₄/H₂ gas mixture (1000 sccm/400 sccm) was then flowed into the reactor for 10 minutes. After growth, the chamber was cooled to room temperature under an Ar environment.

Choi W.J., Chung Y.J., Kim Y.H., Han J., Lee Y.K., Kong K.J., Chang H., Lee Y.K., Kim B.G, & Lee J.O. (2014). Drawing Circuits with Carbon Nanotubes: Scratch-Induced Graphoepitaxial Growth of Carbon Nanotubes on Amorphous Silicon Oxide Substrates. Scientific Reports, 4, 5289.

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Fabrication of Fiber-based Immunoassay

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The silicon core polymer clad optical fiber (400 µm, multimode) was purchased from Thorlabs. Ferritin monoclonal antibodies were purchased from Thermo Fisher, India. IgG from human serum (salt-free, lyophilized powder), Ferritin (equine spleen), and Rabbit Anti-Human IgG polyclonal antibodies were purchased from Sigma. All other chemicals including Molybdenum disulphide (MoS₂, < 2 µm) were high purity grade materials from Sigma/Merck.

Thawany P., Khanna A., Tiwari U.K, & Deep A. (2023). L-cysteine/MoS2 modified robust surface plasmon resonance optical fiber sensor for sensing of Ferritin and IgG. Scientific Reports, 13, 5297.

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