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Superdex 75 increase column

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Superdex 75 Increase column is a prepacked size exclusion chromatography column used for the purification and analysis of proteins, peptides, and other biomolecules. It is designed to provide high-resolution separation of molecules within a molecular weight range of 3,000 to 70,000 Da.

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Lab products found in correlation

Minidawn treos multi angle light scattering detector, by Wyatt Technology (1 mentions) Astra 6, by Wyatt Technology (1 mentions) Ni sepharose excel resin, by Cytiva (1 mentions) Expifectamine, by Thermo Fisher Scientific (1 mentions) Ni sepharose excel, by Cytiva (1 mentions)

Close spelling variants of this product

Superdex 75 Increase 10/300 GL column Superdex 75 10/300 Increase column Superdex 75 Increase Superdex 75 column Superdex 75

6 protocols using superdex 75 increase column

1

Labeling of MBD2-Cys Peptide

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For stopped-flow experiments, 100 μM of the MBD2-Cys peptide in TBS buffer was reduced in 1 mM TCEP and subsequently labeled with 2 mM maleimide-activated dansyl dye (Sigma-Aldrich) at 4 °C overnight, protected from light, and with 15 rpm rolling. The reaction was stopped with 52.7 mM β-mercaptoethanol, and excess dye was removed by SEC in TBS buffer using Superdex 75 Increase column (Cytiva).
Dyla M., González Foutel N.S., Otzen D.E, & Kjaergaard M. (2022). The optimal docking strength for reversibly tethered kinases. Proceedings of the National Academy of Sciences of the United States of America, 119(25), e2203098119.
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2

Size-exclusion chromatography of MAP7 MTBD

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Size-exclusion chromatography of the MAP7 MTBD was performed on a Shimadzu UFLC with a Superdex 75 Increase column (Cytiva), calibrated with 40 mM phosphate buffer, 150 mM NaCl, 1 mM dithiothreitol (DTT), pH 6.5, and coupled to a miniDAWN TREOS multi-angle light scattering detector (Wyatt) and a RID-10 A differential refractive index monitor (Shimadzu). 2 mg/mL ovalbumin was used as a standard to perform signal alignment and normalization. 0.8, 1.6, and 3.2 mg/mL MAP7 MTBD were injected, and collected data was analyzed using ASTRA6 software (Wyatt).
Adler A., Bangera M., Beugelink J.W., Bahri S., van Ingen H., Moores C.A, & Baldus M. (2024). A structural and dynamic visualization of the interaction between MAP7 and microtubules. Nature Communications, 15, 1948.
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3

Expression and Purification of Pfs230D1 Variants

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For binding study, Pfs230D1 (amino acid 542–676) variants were expressed in Expi293 cells as secreted proteins with 6xHis-tag at C-terminus. After 5 days of expression, the culture medium was mixed with Ni Sepharose Excel resin (Cytiva, Marlborough, USA). The resin was washed with Buffer A (25 mM Tris pH 7.4, 0.3 M NaCl) supplemented with 30 mM imidazole. Proteins were eluted with Buffer A supplemented with 150 mM imidazole. Eluate was concentrated and injected onto Superdex 75 Increase column (Cytiva, Marlborough, USA) equilibrated with 20 mM Tris. pH 8, 100 mM NaCl. Fractions were pooled and stored at −80°C. For crystallization, recombinant Pfs230D1 protein was expressed in Pichia pastoris as previously described 24 (link). Pfs230D1D2 (amino acid 542–886) was expressed in Expi293 cells as secreted proteins with 6xHis-tag at C-terminus.
Tang W.K., Coelho C.H., Miura K., Nguemwo Tentokam B.C., Salinas N.D., Narum D.L., Healy S.A., Sagara I., Long C.A., Duffy P.E, & Tolia N.H. (2023). A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine. Immunity, 56(2), 433-443.e5.
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4

Production and Purification of scFvs

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The variable segment of the heavy chain sequence of hmAbs were fused to the light chain variable segment by (GGGGS)4 linker and cloned into the vector pHLsec. The plasmids were transfected into Expi293 cells with ExpiFectamine (Thermo Fisher Scientific, Waltham, USA) according to manufacturer’s protocol. All recombinant scFvs were expressed as secreted proteins. The culture medium was loaded into Ni Sepharose Excel (Cytiva, Marlborough, USA) column and the resin was washed with Buffer A (25 mM Tris pH 7.4, 0.3 M NaCl) supplemented with 30 mM imidazole. The scFvs were eluted with Buffer A supplemented with 150 mM imidazole. Eluate was concentrated and injected onto Superdex 75 Increase column (Cytiva, Marlborough, USA) equilibrated with 20 mM Tris pH 8, 100 mM NaCl. Fractions were pooled and stored at −80°C.
Tang W.K., Coelho C.H., Miura K., Nguemwo Tentokam B.C., Salinas N.D., Narum D.L., Healy S.A., Sagara I., Long C.A., Duffy P.E, & Tolia N.H. (2023). A human antibody epitope map of Pfs230D1 derived from analysis of individuals vaccinated with a malaria transmission-blocking vaccine. Immunity, 56(2), 433-443.e5.
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5

Protein Purification via HPLC

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Each labeled protein was separated from free dye using an HPLC system with a Superdex 75 increase column (Cytiva). First, the column was equilibrated with 50 ml of standard buffer (20 mM HEPES pH 7.8, 150 mM NaCl). Next, the labeled samples were eluted within one column volume using the same buffer. The collected fractions were stored at 4 °C for the experiments. For the case of unlabeled ZIP-lin and ZIP-lin-FKH proteins, an equilibrated aliquot of each construct was run using the same mentioned buffer.
Cruz P., Paredes N., Asela I., Kolimi N., Molina J.A., Ramírez-Sarmiento C.A., Goutam R., Huang G., Medina E, & Sanabria H. (2023). Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1. The Journal of Chemical Physics, 158(19), 195101.
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6

Labeling MBD2-Cys Peptide with Dansyl Dye

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For stopped-flow experiments, 100 μM of the MBD2-Cys peptide in TBS buffer was reduced in 1 mM TCEP, and subsequently labelled with 2 mM maleimide-activated Dansyl dye (Sigma-Aldrich) at 4°C overnight, protected from light, and with 15 rpm rolling. The reaction was stopped with 52.7 mM BME, and excess dye was removed by SEC in TBS buffer using Superdex 75 Increase column (Cytiva).
Dyla M., Foutel N.S.G., Otzen D.E., & Kjærgaard M. (2022). The optimal docking strength for reversibly tethered kinases.
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