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T rex refractive index detector

Manufactured by Wyatt Technology
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The T-rEX is a refractive index detector designed for liquid chromatography applications. It measures the change in refractive index of a sample as it passes through the detector cell, providing a signal that is proportional to the concentration of the analyte.

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Lab products found in correlation

1100 series hplc system, by Agilent Technologies (2 mentions) Heleos 2 multi angle light scattering detector, by Wyatt Technology (2 mentions) Wtc 050n5 size exclusion column, by Wyatt Technology (2 mentions) Astra 7, by Wyatt Technology (2 mentions) Astra software, by Wyatt Technology (1 mentions) 1260 infinity hplc system, by Agilent Technologies (1 mentions) Superdex 200, by GE Healthcare (1 mentions) Dawn heleos 2 mals detector, by Wyatt Technology (1 mentions) Dd2 nmr spectrometer, by Agilent Technologies (1 mentions) Ultimate 3000 uhplc, by Agilent Technologies (1 mentions) Zetasizer pro, by Malvern Panalytical (1 mentions) Dawn heleos 2, by Wyatt Technology (1 mentions) Chromeleon 7.2 chromatography data system software, by Thermo Fisher Scientific (1 mentions) Astra 6, by Wyatt Technology (1 mentions) Ultimate 3000 uhplc system, by Thermo Fisher Scientific (1 mentions)

7 protocols using t rex refractive index detector

1

SEC-MALS Analysis of Protein Samples

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Protein samples to be measured in SEC coupled with MALS were diluted to 0.5 to 1.0 mg/ml in a volume of 70 μl of buffer A without glycerol. About 50 μl were injected using an autosampler onto a Superose 6 increase (10/300) GL column connected to a 1260 Infinity HPLC system (Agilent), running with a flow rate of 0.5 ml/min. The outlet of the column was directly connected to an Optilab T-rEX refractive index detector following a miniDAWN MALS system (Wyatt). Setting baselines and defining peak areas were carried out using the ASTRA software (Wyatt). MW was determined based on the previous assignment in the ASTRA software.
Moecking J., Laohamonthonkul P., Meşe K., Hagelueken G., Steiner A., Harapas C.R., Sandow J.J., Graves J.D., Masters S.L, & Geyer M. (2022). Inflammasome sensor NLRP1 disease variant M1184V promotes autoproteolysis and DPP9 complex formation by stabilizing the FIIND domain. The Journal of Biological Chemistry, 298(12), 102645.
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2

SEC-MALS Characterization of Virus Conjugates

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The multi-angle light scattering coupled with size exclusion chromatography (SEC-MALS) was used to characterize the empty virus capsids and the carbohydrate-virus conjugates. The SEC-MALS system used in this study included the 1100 series HPLC system (Agilent, Santa Clara, CA), the HELEOS-II multi-angle light scattering detector, the TrEX refractive index detector, and the WTC-050N5 size exclusion column (Wyatt Technology, Santa Barbara, CA). Data obtained for the virus-lactose conjugate reaction solution ware analyzed using the ‘protein conjugate’ method in ASTRA 7 software (Wyatt Technology, Santa Barbara, CA) [27 (link)].
For the conjugate analysis of the SEC-MALS data, the averaged refractive index increments of the protein (0.185 mL/g [28 ]) and polysaccharide (0.15 mL/g [29 (link), 30 ]) were used for the virus capsid and the linker-equipped lactose, respectively. The 280 nm UV extinction coefficient of the unconjugated virus capsid was determined by performing the unconjugated capsid sample measurement on the SEC-MALS and analyzing the data using the known protein refractive index increment (0.185 mL/g [28 ]). The 280 nm UV extinction coefficient of the linker-equipped lactose was determined by a spectrophotometer (HP 8453, OLIS Inc., Athens, GA).
Wu D., Xu P., Kelly M., Ryan E.T., Kováč P, & Piszczek G. (2023). Mass photometry: A powerful tool for carbohydrates-proteins conjugation monitoring and glycoconjugates molecular mass determination. Glycoconjugate journal, 40(4), 401-412.
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3

SEC-MALS Characterization of Virus Conjugates

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The multi-angle light scattering coupled with size exclusion chromatography (SEC-MALS) was used to characterize the empty virus capsids and the carbohydrate-virus conjugates. The SEC-MALS system used in this study included the 1100 series HPLC system (Agilent, Santa Clara, CA), the HELEOS-II multi-angle light scattering detector, the TrEX refractive index detector, and the WTC-050N5 size exclusion column (Wyatt Technology, Santa Barbara, CA). Data obtained for the virus-lactose conjugate reaction solution ware analyzed using the 'protein conjugate' method in ASTRA 7 software (Wyatt Technology, Santa Barbara, CA) [27] (link).
For the conjugate analysis of the SEC-MALS data, the averaged refractive index increments of the protein (0.185 mL/g [28] ) and polysaccharide (0.15 mL/g [29, (link)30] ) were used for the virus capsid and the linker-equipped lactose, respectively. The 280 nm UV extinction coefficient of the unconjugated virus capsid was determined by performing the unconjugated capsid sample measurement on the SEC-MALS and analyzing the data using the known protein refractive index increment (0.185 mL/g [28] ). The 280 nm UV extinction coefficient of the linkerequipped lactose was determined by a spectrophotometer (HP 8453, OLIS Inc., Athens, GA).
Wu D., Xu P., Kelly M., Ryan E.T., Kováč P, & Piszczek G. (2023). Mass photometry: A powerful tool for carbohydrates-proteins conjugation monitoring and glycoconjugates molecular mass determination. Glycoconjugate journal, 40(4).
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4

Size Exclusion Chromatography with MALS

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Analytical size exclusion chromatography was carried out on Superdex 200 and Superdex 75 Tricorn 10/300 columns (GE Healthcare), using an Ultimate 3000 SD chromatographic system (Dionex GmbH, Idstein, Germany). For molecular size determination by multiangle laser light scattering (MALS), a MiniDawn TREOS on-line MALS detector and a tREX refractive index detector (Wyatt Technology Europe GmbH, Dernbach, Germany) were coupled to the chromatographic system.
Lorey S., Fiedler E., Kunert A., Nerkamp J., Lange C., Fiedler M., Bosse-Doenecke E., Meysing M., Gloser M., Rundfeldt C., Rauchhaus U., Hänssgen I., Göttler T., Steuernagel A., Fiedler U, & Haupts U. (2014). Novel Ubiquitin-derived High Affinity Binding Proteins with Tumor Targeting Properties. The Journal of Biological Chemistry, 289(12), 8493-8507.
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5

Protein molar mass determination via MALS

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SEC–multi angle light scattering (MALS) was performed using a Shimadzu Prominence HPLC (Kyoto, Japan) equipped with a Shodex KW402.5-4F column (Showa Denko Europe GmbH, Germany) connected to a Dawn Heleos II MALS detector equipped with a 660-nm laser and in-line T-rEX refractive index detector (Wyatt Technology Inc., California, USA). An aliquot of the protein was loaded onto the column and eluted at a flow rate of 0.2 ml per min in PBS buffer. The molar mass of pure protein was calculated from the observed light scattering intensity using a refractive index increment (dn/dc) of 0.185 ml g−1 as implemented in the ASTRA software (Wyatt Technology Inc.).
Egea-Jimenez A.L., Gallardo R., Garcia-Pino A., Ivarsson Y., Wawrzyniak A.M., Kashyap R., Loris R., Schymkowitz J., Rousseau F, & Zimmermann P. (2016). Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled 7 trafficking and signalling. Nature Communications, 7, 12101.
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6

NMR, SEC, and DLS Characterization

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1H NMR spectra were recorded on either a 400 MHz or 500 MHz Agilent DD2 NMR spectrometer. SEC was performed on a ThermoFisher Ultimate 3000 UHPLC equipped with two Agilent InfinityLab PolyPore columns (7.5 × 300 mm) connected in series at 60 °C. Dimethyl formamide (DMF) with 1 g/L LiBr added was used as the eluent at a flow rate of 1 mL/min. The polymer molecular weight was obtained using a T-rEX refractive index detector (Wyatt Technology) and a Dawn Heleos II (Wyatt Technology) eight angle light scattering detector. DLS including zeta potential measurements were performed using a Zetasizer Pro (Malvern Panalytical).
Grundler J., Shin K., Suh H.W., Zhong M, & Saltzman W.M. (2021). Surface Topography of Polyethylene Glycol Shell Nanoparticles Formed from Bottlebrush Block Copolymers Controls Interactions with Proteins and Cells. ACS nano, 15(10), 16118-16129.
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7

Polymer Molecular Weight Analysis

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The number and weight average molecular weights of all polymers were measured by gel permeation chromatography (GPC) driven by the Ultimate 3000 UHPLC system (Thermo Fisher Scientific, Waltham, MA, USA) equipped with a TREX refractive index detector (Wyatt Technologies, Santa Barbara, CA, USA). The instrument was controlled using Chromeleon™ 7.2 Chromatography Data System software (Thermo Fisher Scientific, Waltham, MA, USA) and data collection and analysis was performed in ASTRA 6.0 (Wyatt Technologies, Santa Barbara, CA, USA).
Kauffman A.C., Piotrowski-Daspit A.S., Nakazawa K.H., Jiang Y., Datye A, & Saltzman W.M. (2018). Tunability of Biodegradable Poly(amine-co-ester) Polymers for Customized Nucleic Acid Delivery and Other Biomedical Applications. Biomacromolecules, 19(9), 3861-3873.
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