Mals instrument

Manufactured by Wyatt Technology

Sourced in Germany

The MALS (Multi-Angle Light Scattering) instrument is a laboratory device that measures the light scattering properties of samples. It is designed to determine the molecular weight, size, and shape of macromolecules, such as proteins, polymers, and nanoparticles, in solution.

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Lab products found in correlation

Avance 400, by Bruker (1 mentions) Tsk gel super h h guard, by Tosoh (1 mentions) Tsk gel hm n for gel separation, by Tosoh (1 mentions) Minidawn treos, by Wyatt Technology (1 mentions) Astra software, by Wyatt Technology (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Dawn helios 2, by Wyatt Technology (1 mentions) Optilab t rex, by Wyatt Technology (1 mentions)

Spelling variants of this product

MiniDAWN TREOS MALS instrument (13 citations) DAWN HELEOS-II MALS instrument (7 citations) Wyatt MiniDAWN TREOS MALS instrument (2 citations)

3 protocols using mals instrument

Polymer Characterization via GPC-MALS

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Absolute molecular weights and polydispersities (Mw/Mn, PDI) of all polymers were determined by gel permeation chromatography (GPC, 1200 Series, Shimadzu Technologies, Santa Clara, CA) equipped with a miniDAWN TREOS, multi-angle light scattering (MALS) instrument (Wyatt Technologies, Santa Barbara, CA) and a refractive index detector (Shimadzu Technologies, Santa Clara, CA) [columns: TSK Gel Super H-H guard; TSK Gel HM-N for gel separation, Tosoh Bioscience, Montgomeryville, PA]. HPLC-grade DMF containing 0.05 M LiBr at 60 °C was used as the mobile phase at a flow rate of 0.35 mL/min. Absolute molecular weights were determined using reported dn/dc values for p(DMAEMA) (0.06 ml/g)^{77 –79} and PEG (0.13 ml/g).^{80 (link)} Block copolymers that included pH-responsive blocks ((p(DMAEMA-co-BMA-co-PAA)) were analyzed via¹H NMR spectroscopy (Bruker Avance 400) to confirm second block composition, as previously described.²⁹

Horev B., Klein M.I., Hwang G., Li Y., Kim D., Koo H, & Benoit D.S. (2015). pH-activated Nanoparticles for Controlled Topical Delivery of Farnesol to Disrupt Oral Biofilm Virulence. ACS nano, 9(3), 2390-2404.

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Determining Protein Molar Mass via SEC-MALS

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Size exclusion chromatography (SEC) coupled with multi-angle light scattering (MALS) was performed at room temperature using a Shodex packed HPLC column (Showa Denko Europe GmbH, Germany) connected to a Wyatt Technology MALS instrument. A 50 μl aliquot of protein (spinned for 30 min at 20 000 rpm in a microcentrifuge) was loaded onto the column and eluted at a flow rate of 0.2 ml/min in 20 mM Tris-HCl pH 7.0, 300 mM NaCl. The molar mass of the pure protein was calculated from the observed light scattering intensity using a refractive index (dn/dc) of 0.185 ml/g. The instrument was previously calibrated with bovine serum albumin (BSA) as standard (BSA dimer = 134 kDa and BSA monomer = 66 kDa). The results were analyzed using the ASTRA software (Wyatt Technologies, Inc.).

Zorzini V., Buts L., Sleutel M., Garcia-Pino A., Talavera A., Haesaerts S., Greve H.D., Cheung A., van Nuland N.A, & Loris R. (2014). Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics. Nucleic Acids Research, 42(10), 6709-6725.

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Size Exclusion Chromatography of Purified Nups

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The purified individual Nups and complexes at various concentrations (Supplemental Table S4) were analyzed with SEC using either Superdex 200 10/30 GL or Superose6 increase 10/30 GL column coupled with a MALS instrument (Wyatt Technology). The chromatography system was connected in series with a light-scattering detector (Wyatt Dawn HELIOS II) and refractive index detector (Wyatt Optilab t-rEX). Bovine serum albumin (2 mg/ml) (Sigma) was used as a standard to calibrate the system, and 100 µl of each sample was injected. The column was equilibrated with the SEC buffer. Data analysis was carried out using the program ASTRA (Wyatt Technology), yielding the molar mass and mass distribution (polydispersity) of the samples.

Madheshiya P.K., Shukla E., Singh J., Bawaria S., Ansari M.Y, & Chauhan R. (2022). Insights into the role of Nup62 and Nup93 in assembling cytoplasmic ring and central transport channel of the nuclear pore complex. Molecular Biology of the Cell, 33(14), ar139.

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