Bio gel p 6

Manufactured by Bio-Rad

Sourced in United States

Bio-Gel P-6 is a size exclusion chromatography resin used for the separation and purification of biomolecules. It is a polyacrylamide-based gel that separates molecules based on their size and molecular weight. The resin is available in different fractionation ranges to accommodate a variety of sample types and applications.

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Lab products found in correlation

Micro bio spin column, by Bio-Rad (8 mentions) Bio beads sm 2 resin, by Bio-Rad (2 mentions) 1 2 dioleoyl sn glycero 3 phosphoethanolamine headgroup labeled with atto 488 atto488 pe, by ATTO-TEC (2 mentions) Filtropur, by Sarstedt (2 mentions) Horse heart cytochrome c, by Merck Group (2 mentions) 6530 q tof, by Agilent Technologies (2 mentions) L α phosphatidylcholine egg pc, by Avanti Polar Lipids (1 mentions) Alexa 680 c2 maleimide, by Thermo Fisher Scientific (1 mentions) Qtof2, by Waters Corporation (1 mentions) Sequencing grade trypsin, by Promega (1 mentions) Iodoacetamide, by Merck Group (1 mentions) Quant it picogreen dsdna assay kit, by Thermo Fisher Scientific (1 mentions) Epmotion 5075 tmx, by Eppendorf (1 mentions) Lightcycler 480 system, by Roche (1 mentions) Geneclean turbo kit, by MP Biomedicals (1 mentions) Masshunter b 07, by Agilent Technologies (1 mentions) Recombinant hel, by Merck Group (1 mentions) Biogel p10, by Bio-Rad (1 mentions) Bio gel p 4, by Bio-Rad (1 mentions) Poly a purist kit, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Micro Bio-Spin™ P-6 Gel Columns (45 citations) Bio-Gel P-6 column (9 citations) Bio-Gel P-6 desalting cartridge (5 citations) Bio-Spin P-6 Gel Columns (4 citations) Bio-Scale™ Mini Bio-Gel® P-6 Desalting Cartridge (4 citations) Micro bio-spin columns with bio-gel P-6 (3 citations) Bio-Gel P-6 gel column (3 citations) Micro bio-spin gel p-6 columns (2 citations) Bio‐Gel P‐6 spin column (2 citations) Bio-Gel P-6 DG Media (2 citations)

29 protocols using bio gel p 6

Disulfide Bond Detection in mTRPA1

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For disulphide bond detection, purified mTRPA1 channel (50 μM) was first treated with 1 mM DTT and subsequently purified using Micro Bio-Spin Columns with Bio-Gel P-6 (Bio-Rad). The protein was then exposed to either 500 μM or 1.5 mM AS for 15 min, while a sample that was first modified with IA to block all the available SH groups before application of 1.5 mM AS was used as negative control. The samples were desalted on Micro Bio-Spin Columns with Bio-Gel P-6 (Bio-Rad) and processed as follows: (i) 5 mM IA (45 min at 37 °C), (ii) 1 mM DTT (1 h at 37 °C) and (iii) 5 mM biotin-maleimide (45 min at 37 °C). The presence of biotinylated proteins was confirmed with mouse monoclonal anti-biotin peroxidase-labelled antibodies (Clone BN-34, A0184, Sigma-Aldrich).

Eberhardt M., Dux M., Namer B., Miljkovic J., Cordasic N., Will C., Kichko T.I., de la Roche J., Fischer M., Suárez S.A., Bikiel D., Dorsch K., Leffler A., Babes A., Lampert A., Lennerz J.K., Jacobi J., Martí M.A., Doctorovich F., Högestätt E.D., Zygmunt P.M., Ivanovic-Burmazovic I., Messlinger K., Reeh P, & Filipovic M.R. (2014). H2S and NO cooperatively regulate vascular tone by activating a neuroendocrine HNO–TRPA1–CGRP signalling pathway. Nature Communications, 5, 4381.

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Lipid Labeling and Purification for Vesicle Studies

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L-α-phosphatidylcholine (egg PC), 1-palmitoyl-2-{6-[(7-nitro-2–1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-phosphocholine (C6-NBD-PC), and 1,2-dioleoyl-sn-glycero-3-phosphoetholamine-N-(cap biotinyl) (biotin-PE) were obtained from Avanti Polar Lipids Inc. (Birmingham, AL, USA). 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine headgroup labeled with ATTO 488 (ATTO488-PE) was obtained from ATTO-TEC GmbH (Siegen, Germany). Bio-Beads SM-2 Resin and Bio-Gel P-6 were obtained from Bio-Rad Laboratories Inc. (Hercules, CA, USA). Unless indicated otherwise, all other chemicals and reagents were obtained from Sigma-Aldrich (München, Germany). Protease inhibitor cocktail contained aprotinin (5 mg), leupeptin (5 mg), pepstatin (5 mg), antipain (25 mg) and benzamidine (785 mg) in 5 ml DMSO used at 1:1,000 dilution. All buffers and solutions used for vesicles were filter-sterilized through a polyethersulfone membrane with a pore size of 0.2 µm (Filtropur, Sarstedt AG & Co. KG, Nümbrecht, Germany).

Mathiassen P.P., Menon A.K, & Pomorski T.G. (2021). Endoplasmic reticulum phospholipid scramblase activity revealed after protein reconstitution into giant unilamellar vesicles containing a photostable lipid reporter. Scientific Reports, 11, 14364.

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Fluorescent Labeling of Cytochrome P450 Reductase

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Full-length human CPR was expressed, purified, and stored as previously reported.¹⁶ After purification, CPR was labeled with Alexa 680 C₂ Maleimide (Thermo Fisher Scientific, Waltham, MA). Briefly, Alexa 680 C₂ Maleimide was dissolved in 100% HPLC grade acetonitrile, stored at −20 °C in the dark, and used in the following 24 h. CPR was diluted to 15 μM in 100 mM HEPES (pH 7.4) buffer containing 150 mM NaCl and 20% glycerol (v/v). The solution was transferred to a sealed glass vial and gently degassed for 5 min under Ar while kept on ice. The dye was added to the degassed protein containing solution in a 1:1.2 protein:dye concentration ratio and allowed to react under gentle stirring at 4 °C overnight while protecting the reaction mixture from light. The reaction was stopped by addition of a 1 M solution of DTT to a final concentration of 3 mM. The labeled CPR was then purified from the excess dye by using a desalting Micro Bio-Spin column packed with Bio-Gel P-6 (BioRad, Hercules, CA). The gel in the column was suspended in Tris buffer (pH 7.4) but was exchanged with 100 mM HEPES (pH 7.4) containing 140 mM NaCl and 5 mM CaCl₂ (referred to as ER buffer). The degree of labeling was calculated according to the protocol and estimated to be 1. The labeled CPR was then aliquoted, flash frozen in liquid N₂, and stored at −80 °C.

Martinez M.J., Carder J.D., Taylor E.L., Jacobo E.P., Kang C, & Brozik J.A. (2022). Thermodynamic Driving Forces of Redox-Dependent CPR Insertion into Biomimetic Endoplasmic Reticulum Membranes. The journal of physical chemistry. B, 126(8), 1691-1699.

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Production of Hyperoxidized Peroxiredoxin Variants

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Preparation of hyperoxidized Prx2 and Prx3 variants was performed at 1 mg/mL (46 µM) Prx in 20 mM HEPES pH 7.5, 100 mM NaCl with volumes ranging from 0.1 to 50 mL. Prx solutions were treated with DTT (50 mM) for 5 min, and H₂O₂ was added to a final concentration of either 0.2 mM (Prx2 WT and mutants), 2.0 mM (Prx3 WT and tail mutants), or 6 mM (Prx3-EE mutant). The resulting solution was incubated for 30 min at 30 °C with mixing at 100 rpm. A 40 μL aliquot was removed at different time points, desalted using a Bio-Gel P6 spin column (Bio-Rad) pre-equilibrated with 0.1% formic acid, and analyzed by Electrospray Ionization Time-of-Flight mass spectrometry (ESI-TOF MS) to monitor the oxidation of Prx-C_P-SH to Prx-C_P-SO₂H. Additional H₂O₂ aliquots were added as needed to continue Prx cycling until most of the Prx-C_P-SH was consumed while minimizing the amount of Prx-C_P-SO₃H formed.

Forshaw T.E., Reisz J.A., Nelson K.J., Gumpena R., Lawson J.R., Jönsson T.J., Wu H., Clodfelter J.E., Johnson L.C., Furdui C.M, & Lowther W.T. (2021). Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants, 10(6), 946.

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Measuring Cytochrome c Reduction and CcP Activity

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This activity was assayed as described (Yonetani and Ray, 1966 (link)). Briefly, 50 mg of horse heart cytochrome c (Merck) were dissolved in 2 mL of 10 mM potassium phosphate pH 7.0 and 1 mM EDTA. To reduce ferricytochrome c, the reaction mixture was incubated with 10 mM sodium dithionite for 2 min. The salt excess was removed by gel filtration in Micro Bio-Spin columns (BioRad) packed with Bio-GelP6 (molecular exclusion limit of 1-6 kDa) (BioRad). Reduced cytochrome c was estimated spectrophotometrically at 550 nm. An aliquot of 10 μL was mixed with 490 μL of phosphate buffer pH 7.0 and absorbance was measured at 550 nm. The absorbance of a ferricyanide-oxidized cytochrome c was also determined. The percentage of cytochrome c reduction was estimated according to Matthis and Erman (1995) (link) using an extinction coefficient (𝜀) of 27.7 mM^-1 cm^-1. To measure CcP activity, the reaction mixture (500 μL) contained 10 mM potassium phosphate pH 7.0, 25 mM ferrocytochrome c, and 50 μg protein extract. The reaction was started by adding 200 mM H₂O₂. The enzyme assay was performed by measuring the oxidation rate of ferrocytochrome c every 10 s for 3 min.

Ferrer A., Rivera J., Zapata C., Norambuena J., Sandoval Á., Chávez R., Orellana O, & Levicán G. (2016). Cobalamin Protection against Oxidative Stress in the Acidophilic Iron-oxidizing Bacterium Leptospirillum Group II CF-1. Frontiers in Microbiology, 7, 748.

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Native Mass Spectrometry of Protein-Nucleotide Complexes

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Protein samples were exchanged to a buffer containing 150 mM ammonium acetate pH 7.5 using micro Bio-spin columns (Bio-gel P6, Bio-rad). For measurements in the presence of nucleotide (GDP or GppNHp), samples were pre-incubated with 500 µM nucleotide and 100 µM nucleotide was added to the ammonium acetate buffer. Final protein concentrations ranged between 12.5 and 16 µM. Samples were introduced into the vacuum of the mass spectrometer using nanoelectrospray ionization with in-house-prepared, gold-coated borosilicate glass capillaries with a spray voltage of +1.4 kV. Spectra were recorded on a quadrupole TOF instrument (Q-TOF2, Waters) modified for transmission of native, high-m/z protein assemblies, as described elsewhere^{56 (link)}. Critical voltages and pressures throughout the instrument were 120 and 25 V for the sampling cone and collision voltage respectively, with pressures of 10 and 2E−2 mbar for the source and collision cell.

Deyaert E., Wauters L., Guaitoli G., Konijnenberg A., Leemans M., Terheyden S., Petrovic A., Gallardo R., Nederveen-Schippers L.M., Athanasopoulos P.S., Pots H., Van Haastert P.J., Sobott F., Gloeckner C.J., Efremov R., Kortholt A, & Versées W. (2017). A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nature Communications, 8, 1008.

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HDAC8 Inhibition Assay Protocol

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HDAC8_wt in storage buffer containing (pH 8.0, 150 mm KCl, 50 mm Tris, 25 % glycerol, 1 mm TCEP) was buffer exchanged to 10 mm NH₄HCO₃ pH 8.0 with mini GPC column (self‐packed Bio Gel‐P6, Biorad) at 1020 g for 4 min. Buffer exchanged samples containing 25.5 μm HDAC8 were treated with no inhibitor and 25‐fold excess (637 μm) PD‐404,182 (TOCRIS) for 1 h at 30 °C followed by protein precipitation with 10 % TCA (see EMSA section). Precipitated protein was resuspended in 10 mm NH₄HCO₃ containing 5 m guanidine and 10 mm iodoacetamide (Merck). Alkylation was performed at 22 °C for 20 min under exclusion of light followed by desalting with mini GPC columns. Samples were tryptic digested with 5 μg (50 ng μL⁻¹) in 10 mm NH₄HCO₃ activated trypsin sequencing grade (Promega) for 3 h at 37 °C and 550 rpm. Reaction was stopped by addition of 1 % FA (VWR) and prior to injection centrifugated at 18 000 g for 10 min. 10 μL Supernatant was used for HPLC‐MS injection.

Jänsch N., Sugiarto W.O., Muth M., Kopranovic A., Desczyk C., Ballweg M., Kirschhöfer F., Brenner‐Weiss G, & Meyer‐Almes F. (2020). Switching the Switch: Ligand Induced Disulfide Formation in HDAC8. Chemistry (Weinheim an Der Bergstrasse, Germany), 26(58), 13249-13255.

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Labeling Membrane Proteins from Dendritic Cells

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Membrane proteins were extracted from iDCs, tDCs, niDCs, and ntDCs using a commercial protein extraction kit (Mem-Per^®, Thermo Fisher Scientific). Proteins recovered from 10⁶ cells were labeled with 100 µg (10 mg/mL in DMSO) Alexa Fluor^® succinimidyl ester 555 dye (Thermo Fisher Scientific) as per the manufacturer’s instructions. Labeled protein was separated from unconjugated dye with Bio-Gel^® P6 (Bio-Rad Laboratories, Dublin, Ireland).

Lynch K., Treacy O., Gerlach J.Q., Annuk H., Lohan P., Cabral J., Joshi L., Ryan A.E, & Ritter T. (2017). Regulating Immunogenicity and Tolerogenicity of Bone Marrow-Derived Dendritic Cells through Modulation of Cell Surface Glycosylation by Dexamethasone Treatment. Frontiers in Immunology, 8, 1427.

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Soil and Stem DNA Extraction

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DNA extracts were filtered through PVPP (PolyVinylPolyPyrrolidone) Micro Bio-Spin® Columns with Bio-Gel® P-6 (Bio-Rad) by a 4 min at 1,000 g, 10°C centrifugation. Collected samples were then purified using the Geneclean Turbo kit (MP-Biomedicals, NY, USA) following the manufacturer's instructions. DNA was quantified on a LightCycler 480 System (Roche) using the Quant-iT™ PicoGreen® dsDNA Assay kit (Invitrogen). Samples were normalized to a concentration of 5 ng/μl and the DNA from the five replicates pooled using the epMotion® 5075 TMX (eppendorf). Altogether, 16 soil samples and 14 stem samples were recovered for further analysis.

Djemiel C., Grec S, & Hawkins S. (2017). Characterization of Bacterial and Fungal Community Dynamics by High-Throughput Sequencing (HTS) Metabarcoding during Flax Dew-Retting. Frontiers in Microbiology, 8, 2052.

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Thiolation of Telomeric Repeat Factor

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The thiolation of TRF was performed according to the literature with modifications [15 (link)]. A diluted solution of TCEP (5.7 µg/mL) in 0.1 M phosphate buffer at pH = 7.4 was prepared. Then, 2-iminothiolane was dissolved in this solution at various concentrations (ranging from 3.5 μg/mL to 14.0 µg/mL). To dissolve 1 mg TRF, 1 mL of this solution was employed and was kept reacting for 1 hour. Three different 2-iminothiolane/TRF molar ratios were employed: 2:1, 4:1, and 8:1. The TRF-SH underwent purification through size exclusion (Biogel P-6, BioRad, Hercules, CA, USA) and characterization through electrophoresis.

Muntoni E., Martina K., Marini E., Giorgis M., Lazzarato L., Salaroglio I.C., Riganti C., Lanotte M, & Battaglia L. (2019). Methotrexate-Loaded Solid Lipid Nanoparticles: Protein Functionalization to Improve Brain Biodistribution. Pharmaceutics, 11(2), 65.

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