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Biorex 70 resin

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Biorex-70 resin is a strong cation exchange resin used for the purification and separation of biomolecules. It is composed of a cross-linked polystyrene matrix with sulfonic acid functional groups. The resin is designed for high-performance liquid chromatography (HPLC) applications and can be used to purify a wide range of biomolecules, including proteins, peptides, and nucleic acids.

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Lab products found in correlation

Amylose resin, by New England Biolabs (2 mentions) Turbofect, by Thermo Fisher Scientific (2 mentions) Ni2 nta resin, by Merck Group (1 mentions) Cdna synthesis kit, by Thermo Fisher Scientific (1 mentions) Sybr green mix, by Roche (1 mentions) Protein g beads, by Merck Group (1 mentions) Taq polymerase, by Merck Group (1 mentions) Cell culture plasticware, by Corning (1 mentions) Lb media, by HiMedia (1 mentions) Cell culture chemicals, by Merck Group (1 mentions)

4 protocols using biorex 70 resin

1

Protein Purification and Characterization

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All chemicals were of analytical grade and were purchased from Sigma-Aldrich (USA), Qualigens (India), Merck (India), Himedia (India) and SRL (India). LB media was purchased from Himedia (India). Ni+2-NTA resin, Protein G beads and Taq polymerase were purchased from Merck-Millipore (USA). cDNA synthesis kit was purchased from Thermo-Fisher (USA). Biorex-70 resin was purchased from Bio-Rad (USA). Cell culture chemicals were purchased from Sigma-Aldrich (USA) while cell culture plasticware was from Corning (USA). SYBR Green mix was purchased from Kapa Biosystems (USA).
Rakesh R., Chanana U.B., Hussain S., Sharma S., Goel K., Bisht D., Patne K., Swer P.B., Hockensmith J.W, & Muthuswami R. (2021). Altering mammalian transcription networking with ADAADi: An inhibitor of ATP-dependent chromatin remodeling. PLoS ONE, 16(5), e0251354.
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2

Purification and Characterization of Histones

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Linker histone H1(0) from Xenopus laevis (here referred to as H1) and the double cysteine mutant (H1G101CK195C) were expressed in bacterial cells BL21(DE3) using the plasmid pET3aH1(0)a (25 (link)). Briefly, the coding sequence of H1 was inserted into pET3a vector (Novagen) and linker histones were purified by ion-exchange chromatography using Biorex-70 resin (Bio-Rad) as described (25 (link)). H1 concentration was determined by quantitative comparison with an H1 standard, whose concentration had been determined by amino acid analysis (25 (link)).
All histone H3 (including H3 tail mutants) used for this study contained a cysteine to alanine substitution at position 110. Histone H3 and H4 were expressed in bacterial cells BL21(DE3). Expression and purification of H3 and H4 was performed as described previously (40 (link)), except for the H4 N tail deletion mutant, which was cultured at 30°C. Purified H3/H4 tetramer concentration was determined by quantitative comparison with standard H3/H4 tetramer.
Histone H2A and H2B, including the tail deletion mutants, were expressed in bacterial cells BL21(DE3). Expression and purification of H2A/H2B dimer was performed as described before (41 (link)). H2A/H2B dimer concentration was determined by quantitative comparison with standard tetramer.
Hao F., Murphy K.J., Kujirai T., Kamo N., Kato J., Koyama M., Okamato A., Hayashi G., Kurumizaka H, & Hayes J.J. (2020). Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain. Nucleic Acids Research, 48(20), 11510-11520.
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3

Purification of Wild-type and Mutant BRCA2

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Wild-type and mutant human BRCA2 cDNAs were cloned into the C-terminal MBP-GFP-tagged phCMV1 expression plasmids and purified as described (18 (link), 19 (link)). Briefly, 10 × 15-cm plates of HEK293 cells were transiently transfected using TurboFect (Thermo Scientific) following the manufacturer specifications and harvested 30 hours post-transfection. Cell extracts were bound to Amylose resin (NEB), and the protein was eluted with 10 mM maltose. The eluate was further purified by ion exchange using BioRex 70 resin (BIO-RAD) and step eluted at 250mM, 450 mM, and 1M NaCl (18 (link), 19 (link)). Each fraction was tested for nuclease contamination. The 1M NaCl fractions were used for the DNA binding assay because they were free of nuclease contamination.
Shimelis H., Mesman R.L., Von Nicolai C., Ehlen A., Guidugli L., Martin C., Calléja F.M., Meeks H., Hallberg E., Hinton J., Lilyquist J., Hu C., Aalfs C.M., Aittomäki K., Andrulis I., Anton-Culver H., Arndt V., Beckmann M.W., Benitez J., Bogdanova N.V., Bojesen S.E., Bolla M.K., Borresen-Dale A.L., Brauch H., Brennan P., Brenner H., Broeks A., Brouwers B., Brüning T., Burwinkel B., Chang-Claude J., Chenevix-Trench G., Cheng C.Y., Choi J.Y., Collée M., Cox A., Cross S.S., Czene K., Darabi H., Dennis J., Dörk T., dos-Santos-Silva I., Dunning A.M., Fasching P.A., Figueroa J., Flyger H., García-Closas M., Giles G.G., Glendon G., Guénel P., Haiman C.A., Hall P., Hamann U., Hartman M., Hogervorst F.B., Hollestelle A., Hopper J.L., Ito H., Jakubowska A., Kang D., Kosma V.M., Kristensen V., Collaborators F.N., Lai K.N., Lambrechts D., Le Marchand L., Li J., Lindblom A., Lophatananon A., Lubinski J., Machackova E., Mannermaa A., Margolin S., Marme F., Matsuo K., Miao H., Michailidou K., Milne R.L., Muir K., Neuhausen S.L., Nevanlinna H., Olson J.E., Olswold C., Oosterwijk J.J., Osorio A., Peterlongo P., Peto J., Pharoah P.D., Pylkäs K., Radice P., Rashid M.U., Rhenius V., Rudolph A., Sangrajrang S., Sawyer E.J., Schmidt M.K., Schoemaker M.J., Seynaeve C., Shah M., Shen C.Y., Shrubsole M., Shu X.O., Slager S., Southey M.C., Stram D.O., Swerdlow A., Teo S.H., Tomlinson I., Torres D., Truong T., van Asperen C.J., van der Kolk L.E., Wang Q., Winqvist R., Wu A.H., Yu J.C., Zheng W., Zheng Y., Leary J., Walker L., Foretova L., Fostira F., Claes K.B., Varesco L., Moghadasi S., Easton D.F., Spurdle A., Devilee P., Vrieling H., Monteiro A.N., Goldgar D.E., Carreira A., Vreeswijk M.P, & Couch F.J. (2017). BRCA2 hypomorphic missense variants confer moderate risks of breast cancer. Cancer research, 77(11), 2789-2799.
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4

Purification of Human BRCA2 Fragments

Cited 1 time
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Wild-type and mutant human 2×MBP-BRCA2NTD fragment (BRCA2 aa 250–500) cDNAs were purified as described previously28 (link). Briefly, 10 × 15-cm plates of HEK293 cells were transiently transfected using Turbo-Fect (Thermo Scientific) following the manufacturer’s specifications and harvested 30 h post-transfection. Cell extracts were bound to amylose resin (NEB), and the protein was eluted with 10 mM maltose. The eluate was further purified by ion exchange using BioRex 70 resin (Bio-Rad) and step eluted at 250, 450, and 1 mM NaCl. Each fraction was tested for nuclease contamination. The CTD of BRCA2 and RAD51 were purified as described before28 (link) Only the nuclease-free fractions were used for EMSA or DNA strand exchange assays.
RPA was expressed from plasmid p11d-tRPA (kind gift from Marc Wold) in BL21(DE3) cells (Novagen) and purified as described64 (link).
Vugic D., Dumoulin I., Martin C., Minello A., Alvaro-Aranda L., Gomez-Escudero J., Chaaban R., Lebdy R., von Nicolai C., Boucherit V., Ribeyre C., Constantinou A, & Carreira A. (2023). Replication gap suppression depends on the double-strand DNA binding activity of BRCA2. Nature Communications, 14, 446.
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