Chelex 100 chelating resin

Manufactured by Bio-Rad

Sourced in United States

Chelex 100 is a chelating resin that selectively binds metal ions. It is composed of styrene divinylbenzene copolymer beads containing paired iminodiacetate ions, which act as chelating groups. This resin is primarily used for the purification and concentration of metal ions from aqueous solutions.

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20 protocols using chelex 100 chelating resin

Removing Iron from FreeStyle 293 Media

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To remove Fe in commercial FreeStyle 293 media, 20 g of Chelex 100 chelating resins (Bio-Rad) were added per 1 L and incubated under stirring at 4 °C for 5 days. Media were sterile-filtered after the treatment. ⁵⁷FeCl₃ stock was prepared by dissolving ⁵⁷Fe powder (Isoflex) in 0.1 N HCl. 20 μM of sterile-filtered FeCl₃ solution together with apo-transferrin were added to the treated media. Other essential divalent metal ions, including Mg²⁺ and Ca²⁺, which were also removed by the chelating resins, were supplemented to the treated media per the previous report on the metal contents of FreeStyle 293 media (Richardson et al. 2018 (link)). The media were pH-adjusted with NaOH or HCl to pH = 7.4. Despite the replenishment of essential metal ions, the treated media do not sustain continuous growth of HEK cells. To minimize cell death, culture media were not exchanged until viral transduction. About 16 h after viral transduction, cells in normal media were pelleted at 800xg and resuspended in the treated media with 10 mM sodium butyrate. Then, the suspended cells were incubated at 30 °C for 2 days before harvest. Purification was conducted as described above for normal SCD1.

Shen J., Wu G., Pierce B.S., Tsai A.L, & Zhou M. (2023). Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1. bioRxiv.

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Optimizing HEK Cell Viral Transduction

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To remove Fe in commercial FreeStyle 293 media, Chelex 100 chelating resins (Bio-Rad) were added at 20 g per 1 L and incubated under stirring at 4 °C for 5 days. Media were sterile-filtered after the treatment. ⁵⁷FeCl₃ stock was prepared by dissolving ⁵⁷Fe powder (Isoflex) in 0.1 N HCl. Twenty millimolar of sterile-filtered FeCl₃ solution together with apo-transferrin was added to the treated media. Other essential divalent metal ions, including Mg²⁺ and Ca²⁺, which were also removed by the chelating resins, were supplemented to the treated media per the previous report on the metal contents of FreeStyle 293 media (63 (link)). The treated media were adjusted with NaOH or HCl to pH = 7.4. Despite the replenishment of essential metal ions, the treated media do not sustain the continuous growth of HEK cells. To minimize cell death, culture media were not changed until after viral transduction. About 16 h after viral transduction, cells in normal media were pelleted at 800×g and resuspended in the treated media with 10 mM sodium butyrate. Then, the suspended cells were incubated at 30 °C for 2 days before harvest. Purification was conducted as described above for the normal SCD1 sample.

Shen J., Wu G., Pierce B.S., Tsai A.L, & Zhou M. (2023). Free ferrous ions sustain activity of mammalian stearoyl-CoA desaturase-1. The Journal of Biological Chemistry, 299(7), 104897.

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Measuring HOCl Sensitivity in E. coli

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The molar HOCl concentration from concentrated sodium hypochlorite (Sigma-Aldrich, catalog no. 425044) was quantified by measuring the A₂₉₂ of the stock solution diluted in 10 mM NaOH. Copper-free MOPS was prepared by removing total metals from MOPS minimal media (Teknova) containing 2 g liter⁻¹ glucose and 1.32 mM K₂HPO₄ by treating prepared media with a universal chelator (Chelex 100 chelating resin; Bio-Rad catalog no. 1421253), filtering sterilizing away the Chelex resin, and adding back the metals normally present in MOPS suspended in metal-free water, except for copper. Overnight cultures of MG1655 and MJG0046 were grown up overnight in MOPS with or without copper. The overnight cultures were normalized to an A₆₀₀ of 0.8 in and diluted to an A₆₀₀ of 0.08 in MOPS minimal medium without copper using the indicated combinations and/or concentrations of HOCl and CuCl₂. Cultures were incubated with shaking at 37°C in a Tecan Infinite M1000 plate reader with the A₆₀₀ being measured every 30 min for 27 h. Sensitivity was subsequently determined by comparing lag-phase extensions (the difference in hours to reach A₆₀₀ ≥ 0.15 from the no HOCl treatment control under the same CuCl₂ condition) for each stress condition.

Derke R.M., Barron A.J., Billiot C.E., Chaple I.F., Lapi S.E., Broderick N.A, & Gray M.J. (2020). The Cu(II) Reductase RclA Protects Escherichia coli against the Combination of Hypochlorous Acid and Intracellular Copper. mBio, 11(5), e01905-20.

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64Cu-Macrin Radiolabeling for PET Imaging

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Metal free buffer solutions were prepared using Chelex® 100 Chelating Resin (100–200 mesh, BioRad). NODA-GA-Macrin (10 μg) was dissolved with acetate buffer (100 μL, 0.1 M, pH 6.0). ~5 mCi (~185 MBq) of ⁶⁴CuCl₂ in 0.1 N HCl was mixed with acetate buffer (0.1 M, pH 8.0) to form ⁶⁴Cu(OAc)₂ and pH was adjusted to ~6. The Macrin was labeled with ⁶⁴Cu at 90 °C for 30 min on a thermomixer (900 rpm). The labeling efficiency was monitored by iTLC showing >99% labeling with a specific activity of 20.5 MBq (554 μCi) ⁶⁴Cu μg⁻¹ Macrin. Trace amounts of unchelated ⁶⁴Cu were removed by EDTA chelation (final concentration ~5 mM) followed by centrifugation (MWCO 10 kDa) at 12k × g for 5 min. The buffer was exchanged to saline, and ⁶⁴Cu-Macrin was sterilized using a 0.22 μm HT Tuffryn Meanbrane string filter (PALL) in ~167 MBq (~4.5 mCi) ⁶⁴Cu-Macrin with ~95% average decay-corrected radiochemical yield (RCY). Radio HPLC and iTLC demonstrated >99% radiochemical purity of ⁶⁴Cu-Macrin.

Kim H.Y., Li R., Ng T.S., Courties G., Rodell C.B., Prytyskach M., Kohler R.H., Pittet M.J., Nahrendorf M., Weissleder R, & Miller M.A. (2018). Quantitative Imaging of Tumor Associated Macrophages and Their Response to Therapy Using 64Cu-Labeled Macrin. ACS nano, 12(12), 12015-12029.

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Calcium Removal from Serum Protocol

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To remove calcium from the serum, 500 ml of FBS was mixed with 20 g of Chelex 100 chelating resin (BioRad, Hercules, CA, USA) [42 (link)]. Calcium ultralow concentration medium and calcium-free DMEM (Nacalai Tesque, Kyoto, Japan) containing 10% Chelex-treated FBS and 110 mg/L sodium pyruvate (Nacalai Tesque) were used. Calcium contamination can occur easily. For the calcium-free medium, a calcium ultralow concentration medium containing 0.1 mM ethylene glycol-bis(2-aminoethylether)-N,N,N',N'-tetraacetic acid (EGTA) (Nacalai Tesque) was used. We gradually reduced the calcium concentration of the medium from 2.2 mM to a calcium ultralow concentration at each cell passage.

, & Kitagawa N. (2022). Antimicrobial peptide nisin induces spherical distribution of macropinocytosis-like cytokeratin 5 and cytokeratin 17 following immediate derangement of the cell membrane. Anatomy & Cell Biology, 55(2), 190-204.

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DOTA Labeling of CR3022-F(ab)2

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CR3022-F(ab)2 was labeled with the chelator dodecane tetra-acetic acid (DOTA) for the attachment of ⁶⁴Cu. Chelex 100 chelating resin (#142–1253, BioRad) was used to prepare two buffers: 0.1M sodium phosphate (pH 7.3) and 0.1M ammonium acetate (pH 5.5). Five grams of Chelex was added to 100ml of each buffer and stirred at room temperature for 1 hour. Buffers were then filter sterilized using 0.22 μM filters. CR3022-F(ab’)2 was buffer exchanged into the prepared 0.1 M sodium phosphate using Zeba columns (ThermoFisher, USA). DOTA-NHS-ester (#B-280, Macrocyclics) was dissolved in dimethyl sulfoxide (DMSO) at a concentration of 10mM. A 1:10 dilution of 1M sodium bicarbonate was made into a tube containing F(ab’)2 in sodium phosphate and 10mM DOTA was added at a molar ratio of 5:1. The tube was mixed and left to rock at 37C for 1.5 hours. The labeled F(ab’)2 was then buffer exchanged into fresh 0.1 M sodium phosphate using a Zeba column.

Madden P.J., Thomas Y., Blair R.V., Samer S., Doyle M., Midkiff C.C., Doyle-Meyers L.A., Becker M.E., Arif M.S., McRaven M.D., Simons L.M., Carias A.M., Martinelli E., Lorenzo-Redondo R., Hultquist J.F., Villinger F.J., Veazey R.S, & Hope T.J. (2022). An immunoPET probe to SARS-CoV-2 reveals early infection of the male genital tract in rhesus macaques. bioRxiv.

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Trace Element Enrichment Protocol

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The zeolite, silica, and resin packing materials were sourced as below: treated zeolite 250–300 μm and 150–250 μm Avoca zeolite μm (Neptune Bio-innovations, Sydney, Australia); silica pellets 500 and 800 μm (Umang pharmatech, Maharashtra, India); silica molecular sieve type X13, 8 × 12 mesh (Fujian Anten Chemical Co. Ltd., Xiamen, China); Chelex-100 chelating resin (Bio-Rad, Gladesville, Australia); silica sand, acid-washed (Sigma-Aldrich, St. Louis, MI, USA).
The resins and minerals prewashed with Milli-Q H₂O were packed into a syringe at 20% (v/v) of the water sample volume. The water sample was manually eluted through the packing materials at approximately 20 mL/min.

Sun A., Stanton J.A., Bergquist P.L, & Sunna A. (2021). Universal Enzyme-Based Field Workflow for Rapid and Sensitive Quantification of Water Pathogens. Microorganisms, 9(11), 2367.

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Radiolabeling of PA-GFP-BaL Virus

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PA-GFP-BaL was labeled with a dodecane tetraacetic acid (DOTA) chelator, which allowed for attachment of ⁶⁴Cu. Two buffers were prepared using a chelating resin to remove all free copper: 0.1 M sodium phosphate buffer (pH 7.3) and 0.1 M ammonium acetate buffer (pH 5.5). Chelex 100 Chelating Resin (5 g, BioRad, Hercules, California) was added to 100 ml of each buffer, incubated with stirring for 1 hour at room temperature, and sterilized by filtration at 0.22 μm. Concentrated virus was resuspended in PBS and a 1:10 volume of 1 M sodium bicarbonate added. DOTA-NHS-ester (Macrocyclics, Dallas, Texas) was dissolved in the 0.1 M sodium phosphate buffer. The two solutions were combined (0.3 mg DOTA-NHS-ester per 500 ng of virus, as detected by p24 assay), and incubated at room temperature on a rocker in the dark. After 30 minutes, the buffer was exchanged for the 0.1 M ammonium acetate using a Zeba column 40K (Thermo Fisher Scientific, Waltham, Massachusetts), wash steps completed per manufacturer’s protocol, and virus (PA-GFP-BaL-⁶⁴Cu) collected and frozen for shipment to Research Imaging Institute at UT Health San Antonio (RII-UTHSA) or New Iberia Research Center (NIRC) at the University of Louisiana at Lafayette.

Taylor R.A., Xiao S., Carias A.M., McRaven M.D., Thakkar D.N., Araínga M., Allen E.J., Rogers K.A., Kumarapperuma S.C., Gong S., Fought A.J., Anderson M.R., Thomas Y., Schneider J.R., Goins B., Fox P., Villinger F.J., Ruprecht R.M, & Hope T.J. (2021). PET/CT targeted tissue sampling reveals virus specific dIgA can alter the distribution and localization of HIV after rectal exposure. PLoS Pathogens, 17(6), e1009632.

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Evaluating MeCP2 Binding at Npy and Bdnf

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Chromatin immunoprecipitation (ChIP) assay was performed as described previously (Kokare et al., 2017 (link); Kyzar et al., 2017 (link)) to examine the level of MeCP2 at the promoters of Npy and Bdnf exon IV. Amygdala tissues were homogenized in PBS and briefly fixed in formaldehyde. The fixed tissue homogenate was resuspended in SDS-lysis buffer for 30 min and sonicated to shear the chromatin to 200–500 base-pairs long DNA fragments. Volumes of chromatin from each sample were separated for chromatin immunoprecipitation using an antibody against MeCP2 (ab2828; Abcam, Cambridge, MA, USA) and for quantifying the amount of DNA in different samples before immunoprecipitation (inputs). For immunoprecipitation, chromatin was resuspended in ChIP dilution buffer along with MeCP2 antibody and Protein A/G PLUS-agarose™ beads (Santa Cruz Biotechnology) and incubated overnight at 4 ⁰C. On the following day, chromatin was washed and isolated using Chelex-100 chelating resin (BioRad). qRT-PCR was performed using SYBR Green qPCR SSO Master Mix (BioRad) and primers specific to Npy and Bdnf exon IV as mentioned above. Fold changes in MeCP2 levels were calculated after normalizing to input using 2^−ΔΔCT method (Livak and Schmittgen, 2001 (link)). Results are presented as mean fold changes (±SEM) with respect to control (AIS group).

Sakharkar A.J., Kyzar E.J., Gavin D.P., Zhang H., Chen Y., Krishnan H.R., Grayson D.R, & Pandey S.C. (2019). Altered amygdala DNA methylation mechanisms after adolescent alcohol exposure contribute to adult anxiety and alcohol drinking. Neuropharmacology, 157, 107679.

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Radiolabeling HIV Virus with Copper-64

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HIV virus was DOTA-labeled as previously described [26 (link),30 (link)]. PA-GFP-BaL was labeled with a dodecane tetraacetic acid (DOTA) chelator, which allowed for attachment of ⁶⁴Cu. Two buffers were prepared using a chelating resin to remove all free copper: 0.1 M sodium phosphate buffer (pH 7.3) and 0.1 M ammonium acetate buffer (pH 5.5). Chelex 100 Chelating Resin (5g, BioRad, Hercules, California) was added to 100 ml of each buffer, incubated with stirring for 1 hour at room temperature, and filtered at 0.22 μm for sterilization. Concentrated virus was resuspended in PBS and a 1:10 volume of 1 M sodium bicarbonate added. DOTA-NHS-ester (Macrocyclics, Dallas, Texas) was dissolved in the 0.1 M sodium phosphate buffer. The two solutions were combined (0.3mg DOTA-NHS-ester per 500ng of virus, as detected by p24 assay), and incubated on a rocker in the dark at room temperature. After 30 minutes, the buffer was exchanged for the 0.1 M ammonium acetate using a Zeba column 40K (Thermo Fisher Scientific, Waltham, Massachusetts), wash steps completed per manufacturer’s protocol, and virus (PA-GFP-BaL-⁶⁴Cu) collected and frozen for shipment to New Iberia Research Center (NIRC) at the University of Louisiana at Lafayette.

Taylor R.A., McRaven M.D., Carias A.M., Anderson M.R., Matias E., Araínga M., Allen E.J., Rogers K.A., Gupta S., Kulkarni V., Lakhashe S., Lorenzo-Redondo R., Thomas Y., Strickland A., Villinger F.J., Ruprecht R.M, & Hope T.J. (2021). Localization of infection in neonatal rhesus macaques after oral viral challenge. PLoS Pathogens, 17(11), e1009855.

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