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Optilab rex differential refractive index detector

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The Optilab rEX differential refractive index detector is a laboratory instrument designed to measure changes in the refractive index of a sample. It operates by comparing the refractive index of the sample to a reference solution, providing a sensitive and accurate method of detection.

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Lab products found in correlation

Superdex 200 10 300 gl column, by GE Healthcare (4 mentions) Astra software, by Wyatt Technology (4 mentions) Superdex 200 increase 10 300 gl column, by GE Healthcare (4 mentions) Dawn helios ii system, by Wyatt Technology (4 mentions) Qels module, by Wyatt Technology (4 mentions) Dawn heleos mals, by Wyatt Technology (4 mentions) Astra 6 software, by Wyatt Technology (4 mentions) Astra 7, by Wyatt Technology (3 mentions) Superdex 200 10 300 increase analytical size exclusion column, by GE Healthcare (2 mentions) Sds page, by Thermo Fisher Scientific (2 mentions) Ettan lc, by GE Healthcare (2 mentions) Minidawn treos light scattering diode array, by Wyatt Technology (2 mentions) Astra 5, by Wyatt Technology (2 mentions) Prism 8, by GraphPad (2 mentions) Astra 6, by Wyatt Technology (2 mentions) Superdex 200 10 300 increase column, by Agilent Technologies (1 mentions) Multi wavelength absorbance detector, by Wyatt Technology (1 mentions) Heleos 2 8 multi angle light scattering detector, by Wyatt Technology (1 mentions) 1260 hplc, by Agilent Technologies (1 mentions) Bsa solution, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Optilab T-rEX differential refractive index detector Optilab rEX differential refractive index Optilab rEX refractive index detector Optilab differential refractive index (dRI) detector Optilab refractive index detector Differential refractive index detector Optilab rEX detector Refractive index detector Optilab rEX

19 protocols using optilab rex differential refractive index detector

1

Static Light Scattering Analysis of EgA1

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Static light scattering experiments were performed at 25°C using a Superdex 200 10/300 GL column (GE HealthCare) attached in-line to a DAWN-HELEOS light scattering detector and an Optilab rEX differential refractive index detector (Wyatt Technology, Santa Barbara, CA, USA). The column was equilibrated with running buffer (PBS 0.1 μm filtered) and the SEC-MALS system was calibrated with a sample of BSA at 1 g/L in the same buffer. Then 100 μL samples of the EgA1 ATTACK at 0.6 g/L in PBS were injected into the column at a flow rate of 0.5 mL/min. Data acquisition and analysis were performed using ASTRA software (Wyatt Technology). Based on numerous measurements on BSA samples at 1 g/L under the same or similar conditions we estimate that the experimental error in the molar mass is around 5%.
Harwood S.L., Alvarez-Cienfuegos A., Nuñez-Prado N., Compte M., Hernández-Pérez S., Merino N., Bonet J., Navarro R., Van Bergen en Henegouwen P.M., Lykkemark S., Mikkelsen K., Mølgaard K., Jabs F., Sanz L., Blanco F.J., Roda-Navarro P, & Alvarez-Vallina L. (2017). ATTACK, a novel bispecific T cell-recruiting antibody with trivalent EGFR binding and monovalent CD3 binding for cancer immunotherapy. Oncoimmunology, 7(1), e1377874.
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2

SEC-MALS Analysis of CckA Receptor

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SEC-MALS measurements for CckARec were performed at a sample loading concentration of 13.8 mg/ml; 6.9 mg/ml and 3.5 mg/ml at 25 C in sample buffer using a GE Healthcare Superdex 200 10/300 Increase column on an Agilent 1260 HPLC. Elution was monitored using an Agilent multi-wavelength absorbance detector (data collected at 280 and 254 nm), a Wyatt Heleos II 8+ multi-angle light scattering detector and a Wyatt Optilab rEX differential refractive index detector. The column was equilibrated overnight in the running buffer to obtain stable baseline signals from the detectors before data collection. Inter-detector delay volumes, band broadening corrections, and light-scattering detector normalization were calibrated using an injection of 2 mg/ml BSA solution (ThermoPierce) and standard protocols in ASTRA 6. Weight-averaged molar mass (Mw), elution concentration, and mass distributions of the samples were calculated using the ASTRA 6 software (Wyatt Technology).
Brüderlin M., Böhm R., Fadel F., Hiller S., Schirmer T, & Dubey B.N. (2023). Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs. Nature Communications, 14, 1002.
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3

Analytical SEC and SEC-MALS of Protein-RNA

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Analytical SEC was performed in buffer M (250 mM NaCl, 20 mM HEPES pH 7.0, 1 mM DTT), or in the appropriate NaCl concentration. Samples were mixed at ∼30 µM and incubated for 15 min in 350 mM NaCl, 20 mM HEPES pH 7.0, 1 mM DTT on ice before being filtered and injected onto a GE Superdex 200 10/300-Increase analytical size exclusion column. When appropriate, samples were mixed with 1.1-fold molar excess RNA. All samples were run at 0.35 mL/min, and peaks were analyzed by SDS-PAGE (Invitrogen). For experiments involving reinjection of fractions over SEC, 500 µL of fractions were spin filtered before reinjecting over SEC.
For SEC-MALS, 165 µg of sample was filtered through a 0.1 µm spin filter (Amicon) before being injected onto a preequilibrated KW-804 column (Shodex). For samples with RNA, stoichiometric amounts of RNA were added prior to spin filtration. Data was acquired with an inline DAWN HELEOS MALS and Optilab rEX differential refractive index detector (Wyatt Technology). All analysis was performed using ASTRA VI software (Wyatt Technology). Data was then exported and plotted with R.
Lobel J.H, & Gross J.D. (2020). Pdc2/Pat1 increases the range of decay factors and RNA bound by the Lsm1–7 complex. RNA, 26(10), 1380-1388.
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4

GR-Loading Complex Formation and Characterization

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Using reaction buffer containing 50 mM HEPES pH 7.5, 50 mM KCl and 2 mM DTT, 10 μM Hsp90 dimer of ATP-binding-deficient mutant (Hsp90(D93N))46 (link), 10 μM Hop, 15 μM Hsp70, 4 μM Hsp40 and 20 μM MBP-GRLBD were incubated with 5 mM ATP/MgCl2 for 1 h at room temperature. The complex was purified and analysed by size-exclusion chromatography with multi-angle light scattering (SEC-MALS) with a Wyatt 050S5 column on an Ettan LC (GE Healthcare) in a running buffer containing 50 mM HEPES, 50 mM KCl, 5 mM MgCl2, 2 mM DTT, 200 μM ADP and 0.01% octyl β-d-glucopyranoside (β-OG). Molecular weights were determined by multi-angle laser light scattering using an in-line DAWN HELEOS and Optilab rEX differential refractive index detector (Wyatt Technology Corporation). Once eluted, fractions containing the GR-loading complex were immediately cross-linked with 0.02% glutaraldehyde for 20 min at room temperature and quenched with 20 mM Tris pH 7.5. Fractions containing the GR-loading complex were separately snap-frozen in liquid nitrogen, and stored in aliquots at −80 °C.
Wang R.Y., Noddings C.M., Kirschke E., Myasnikov A.G., Johnson J.L, & Agard D.A. (2021). Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism. Nature, 601(7893), 460-464.
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5

SEC-MALS Analysis of Ctp1 Protein Complexes

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For SEC-MALS analysis, MBP-Ctp11–60 or MBP-Ctp115–60 proteins in buffer A (25 mM Tris pH 7.5, 200 mM NaCl, 5 mM maltose) or Ctp1 and Ctp11–60 proteins in buffer B (50 mM Tris pH 7.5, 500 mM NaCl, 0.1% β-mercaptoethanol) or Ctp161–294 and Ctp1 R32A K41A in buffer C (25 mM Tris pH 7.5, 200 mM NaCl, 0.1% β-mercaptoethanol) at 2–20 mg ml−1, were run on a Superdex 200 10/300 GL column (GE Healthcare) fit inline with a miniDAWN TREOS light scattering diode array and an Optilab rex differential refractive index detector (Wyatt Technology). Data were analyzed with ASTRA 5.3.4.14 (Wyatt Technology).
Andres S.N., Appel C.D., Westmoreland J., Williams J.S., Nguyen Y., Robertson P.D., Resnick M.A, & Williams R.S. (2015). Tetrameric Ctp1 coordinates DNA binding and bridging in DNA double strand break repair. Nature structural & molecular biology, 22(2), 158-166.
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6

SEC-MALS Analysis of Antibody Proteins

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Static light scattering experiments were performed at room temperature using a Superdex 200 Increase 10/300 GL column (GE Healthcare) attached in-line to a DAWN-HELEOS light scattering detector and an Optilab rEX differential refractive index detector (Wyatt Technology). The column has an exclusion volume of 8.6 ml, and no absorbance (no aggregated protein) was observed in any of the injections. The column was equilibrated with running buffer (PBS+150 Mm NaCl) and the SEC-MALS system was calibrated with a sample of bovine serum albumin (BSA) at 1 g/l in the same buffer. Then 100 μl samples of the two antibodies 1D8N18 and 1D8N/CEGa1 at 1 g/l in the running buffer were injected into the column at a flow rate of 0.5 ml/min. Data acquisition and analysis were performed using the ASTRA software (Wyatt Technology). The reported molar mass corresponds to the center of the chromatography peaks. After separation of the monomeric species by SEC a second injection in the SEC-MALS system was done at 0.26 g/l. Based on numerous measurements on BSA samples at 1 g/l under the same or similar conditions, we estimate that the experimental error in the molar mass is around 5%.
Compte M., Harwood S.L., Muñoz I.G., Navarro R., Zonca M., Perez-Chacon G., Erce-Llamazares A., Merino N., Tapia-Galisteo A., Cuesta A.M., Mikkelsen K., Caleiras E., Nuñez-Prado N., Aznar M.A., Lykkemark S., Martínez-Torrecuadrada J., Melero I., Blanco F.J., Bernardino de la Serna J., Zapata J.M., Sanz L, & Alvarez-Vallina L. (2018). A tumor-targeted trimeric 4-1BB-agonistic antibody induces potent anti-tumor immunity without systemic toxicity. Nature Communications, 9, 4809.
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7

Protein Molecular Mass Determination by SEC-MALS

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Size exclusion chromatography coupled with multi‐angle static light scattering (SEC‐MALS) was performed using an Agilent 1200 series LC system with an online Dawn Helios ii system (Wyatt) equipped with a QELS+ module (Wyatt) and an Optilab rEX differential refractive index detector (Wyatt). 100 μl purified protein from 0.5–2.0 mg/ml was auto‐injected onto a Superdex 200 Increase 10/300 GL column (GE healthcare) and run at 0.5 ml/min. The molecular masses were analysed with ASTRA 7.3.0.11 (Wyatt). Data were plotted using Prism 8.4.3 (GraphPad Software, Inc).
Fischer E.S., Yu C.W., Bellini D., McLaughlin S.H., Orr C.M., Wagner A., Freund S.M, & Barford D. (2021). Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1. EMBO Reports, 22(7), e52242.
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8

SEC-MALS Analysis of LicB Protein

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SEC–multiangle light scattering (MALS) measurements of LicB were performed at 18°C in 10 mM tris-HCl (pH 8.0), 150 NaCl, and 0.012% LMNG using a GE Healthcare Superdex 200 Increase 10/300 GL column on an Agilent 1260 high-performance liquid chromatography. The column was equilibrated overnight for a stable baseline before data collection. Monitoring of the elution was carried out with a multiwavelength absorbance detector at 280 and 254 nm, a Wyatt Heleos II 8+ MALS detector, and a Wyatt Optilab rEX differential refractive index detector. Interdetector delay volumes, light scattering detector normalization, and broadening corrections were calibrated using a bovine serum albumin solution (2 mg/ml; ThermoPierce) and standard protocols in ASTRA 6 (Wyatt Technologies). Weight-averaged molar mass, elution concentration, and mass distribution of the samples were calculated using the ASTRA 6 software (Wyatt Technologies). The specific refractive index increment for the detergent LMNG was assumed to be 0.146 mg/ml according to experimental data.
Bärland N., Rueff A.S., Cebrero G., Hutter C.A., Seeger M.A., Veening J.W, & Perez C. (2022). Mechanistic basis of choline import involved in teichoic acids and lipopolysaccharide modification. Science Advances, 8(9), eabm1122.
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9

SEC-MALS Analysis of Ctp1 Protein Complexes

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For SEC-MALS analysis, MBP-Ctp11–60 or MBP-Ctp115–60 proteins in buffer A (25 mM Tris pH 7.5, 200 mM NaCl, 5 mM maltose) or Ctp1 and Ctp11–60 proteins in buffer B (50 mM Tris pH 7.5, 500 mM NaCl, 0.1% β-mercaptoethanol) or Ctp161–294 and Ctp1 R32A K41A in buffer C (25 mM Tris pH 7.5, 200 mM NaCl, 0.1% β-mercaptoethanol) at 2–20 mg ml−1, were run on a Superdex 200 10/300 GL column (GE Healthcare) fit inline with a miniDAWN TREOS light scattering diode array and an Optilab rex differential refractive index detector (Wyatt Technology). Data were analyzed with ASTRA 5.3.4.14 (Wyatt Technology).
Andres S.N., Appel C.D., Westmoreland J., Williams J.S., Nguyen Y., Robertson P.D., Resnick M.A, & Williams R.S. (2015). Tetrameric Ctp1 coordinates DNA binding and bridging in DNA double strand break repair. Nature structural & molecular biology, 22(2), 158-166.
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10

Hsp27 Oligomerization Analysis

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Solutions of Hsp27 were resolved by analytical SEC on a Shodex 804 column on an Ettan LC (GE Healthcare). Molecular weights were determined by multi-angle laser light scattering using an in-line DAWN HELEOS detector and an Optilab rEX differential refractive index detector (Wyatt Technology Corporation). The column was equilibrated overnight in SEC buffer. Samples were analyzed at the indicated concentrations. Calculation of molecular weights was performed using the ASTRA software package (Wyatt Technology Corporation).
Freilich R., Betegon M., Tse E., Mok S.A., Julien O., Agard D.A., Southworth D.R., Takeuchi K, & Gestwicki J.E. (2018). Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau. Nature Communications, 9, 4563.
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