Superdex 200 column

Manufactured by Wyatt Technology

Sourced in United States

The Superdex 200 column is a size exclusion chromatography column used for the separation and purification of proteins, peptides, and other biomolecules. The column is packed with a cross-linked agarose and dextran matrix that allows for efficient separation based on the size and molecular weight of the analytes.

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Lab products found in correlation

Wyatt dawn heleos 2, by Wyatt Technology (1 mentions) Viscotek 802, by Malvern Panalytical (1 mentions) Omnisize software, by Malvern Panalytical (1 mentions) Superdex 200 10 300 gl column, by GE Healthcare (1 mentions) Astra software, by Wyatt Technology (1 mentions) Astra 6, by Wyatt Technology (1 mentions) Refractive index, by Wyatt Technology (1 mentions)

3 protocols using superdex 200 column

Oligomeric State Determination of DDX1

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The oligomeric state of the protein was determined by static- and dynamic light scattering (SLS/DLS). For SLS 50 μM of DDX1 protein was injected on a Superdex 200 10/300 GL column (GE Healthcare) using a Waters FPLC system (Waters Corp.). The Superdex 200 column was connected to a Wyatt Dawn Heleos II multi-angle-light-scattering (MALS) detector (Wyatt Technology) detecting scattered light from 18 different angles. Refractive index, determined after elution from the column and light scattering data were used to calculate the radius of gyration and the corresponding molecular weight with the help of the Astra Software (Wyatt Technology). For DLS, 25 μM of DDX1 protein in a total volume of 60 μl storage buffer were measured in a Viscotek 802 (Malvern Instruments), which records scattered light at fixed 90° angle. Thirty individual traces with four second measurement time each were recorded. All traces with constant intensity were averaged to fit a combined auto-correlation function, which was used to extract the hydrodynamic radii of the particles in solution and the molecular weight was calculated assuming a globular protein shape. All DLS data analysis was performed using the OmniSIZE Software (Malvern Instruments).

Kellner J.N., Reinstein J, & Meinhart A. (2015). Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1. Nucleic Acids Research, 43(5), 2813-2828.

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Molecular Mass Determination of CHIP Mutants

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The solution molecular weights of WT CHIP, K30A, H260Q and T246M point mutant CHIP were determined by size exclusion chromatography followed by multi-angle light scattering (SEC-MALS) of the eluant from a size exclusion chromatography column. The SEC-MALS system consisted of a GE Superdex 200 column connected to Wyatt DAWN HELEOS-II multi-angle light scattering instrument and a Wyatt T-Rex refractometer (Wyatt Technology, Santa Barbara, CA, USA). 100 μl of 0.5 mg/ml of each sample was loaded onto the column, and the light scattering and refractive index data were collected as the eluted samples passed through light scattering system. The molar masses of the samples eluting in various peaks were calculated from these data using ASTRA 6 software (Wyatt Technology).

Shi C.H., Rubel C., Soss S.E., Sanchez-Hodge R., Zhang S., Madrigal S.C., Ravi S., McDonough H., Page R.C., Chazin W.J., Patterson C., Mao C.Y., Willis M.S., Luo H.Y., Li Y.S., Stevens D.A., Tang M.B., Du P., Wang Y.H., Hu Z.W., Xu Y.M, & Schisler J.C. (2018). Disrupted structure and aberrant function of CHIP mediates the loss of motor and cognitive function in preclinical models of SCAR16. PLoS Genetics, 14(9), e1007664.

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SEC-MALS Analysis of A3B-CTD

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Size-exclusion chromatography/multi-angle light scattering (SEC-MALS) data were obtained at room temperature using an analytical Superdex 200 column with in-line multi-angle light scattering, refractive index (Wyatt Technology, Inc., Santa Barbara, CA), and UV (Agilent Technologies, Santa Clara, CA) detectors. 100 μl of 80 μM A3B-CTD were applied to the column in 25 mM sodium phosphate buffer, pH 6.9, 0.02% sodium azide, and 1 mM DTT at a flow-rate of 0.5 ml/min.

Byeon I.J., Byeon C.H., Wu T., Mitra M., Singer D., Levin J.G, & Gronenborn A.M. (2016). Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. Biochemistry, 55(21), 2944-2959.

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