Superdex 200 5 150 gl

Manufactured by GE Healthcare

Sourced in Japan, United States

The Superdex 200 5/150 GL is a prepacked size exclusion chromatography column designed for fast and efficient separation of proteins, peptides, and other biomolecules. It features a Superdex 200 stationary phase packed in a glass column with a 5 mm inner diameter and 150 mm length. The column is suitable for analytical-scale purification and characterization applications.

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Lab products found in correlation

Linear polyethylenimine, by Polysciences (3 mentions) Deae sepharose ff column, by GE Healthcare (3 mentions) Polyethylenimine (pei), by Polysciences (3 mentions) Protein a column, by GE Healthcare (2 mentions) Pluronic f 68, by Thermo Fisher Scientific (1 mentions) Astra 6, by Wyatt Technology (1 mentions) Ktamicro, by GE Healthcare (1 mentions) Minidawn treos, by Wyatt Technology (1 mentions) Optilab rex, by Wyatt Technology (1 mentions) Superdex 200 increase 10 300 column, by GE Healthcare (1 mentions) Peaq differential scanning calorimeter automated, by Malvern Panalytical (1 mentions) Peaq dsc analysis software, by Malvern Panalytical (1 mentions) 1260 infinity hplc, by Agilent Technologies (1 mentions) Cm10 electron microscope, by Philips (1 mentions) Prominence hplc system, by Shimadzu (1 mentions) Akta purifier, by GE Healthcare (1 mentions) Superose 6 5 150 gl, by GE Healthcare (1 mentions) Histrap ff, by GE Healthcare (1 mentions) Kta system, by GE Healthcare (1 mentions) Superdex 200 10 300 gl, by GE Healthcare (1 mentions)

16 protocols using superdex 200 5 150 gl

Recombinant Antibody Production in HEK293E

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Example 8

The expression and purification of a recombinant antibody protein were conducted by following methods: HEK293E cells cultured in Freestyle 293 Expression Medium with 10% of Pluronic F-68 (Gibco) at 1×10⁶cell/ml were transfected with equal amount of heavy chain vector and light chain vector DNA at final concentration of 0.5 μg/ml and PEI (Polyethylenimine-linear, Polyscience) at 1.0 μg/ml. DNA to PEI ratio was 1:2. DNA and PEI complexes formed period with Optimal MEM should be 15 minutes at the room temperature. Transfected cells were cultured in the flasks with 5% CO2, 37° C. and 125 rpm shaking speed. 1% Peptone medium was added at 22 to 26 hours post transfection. Conditioned medium was harvested on day 6 and supernatant was centrifuged at 3,000 rpm for 30 minutes. The clarified conditioned medium were then loaded onto nProteinA column (G.E. Healthcare), washed with PBS plus 0.1% triton-X100 and finally the bound IgG was eluted with a solution containing 0.1M glycine at pH 3.5. The eluted antibody protein was dialyzed to PBS and stored at −80*C. To remove endotoxin, the purified protein was further processed by passing through Hitrap DEAE Sepharose F.F. column and the resulting antibody was analyzed to determine the level of purity using size exclusion chromatography (Superdex 200 5/150 GL, G.E. Healthcare).

US10233249B2. Antibodies and methods for treating estrogen receptor-associated diseases (2019-03-19). BEIJING SHENOGEN PHARMA GROUP LTD. [CN]. Inventors: Xueming Qian [CN], Kun Meng [CN], Feng Chen [CN], Xiao Shang [CN], Jing Wang [CN], Lu Li [CN], Congya Zhou [CN].

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Multi-angle Light Scattering of VP22core

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Light-scattering data were obtained with analytical size-exclusion chromatography (Superdex 200 5/150 GL; GE Healthcare) coupled with a multi-angle light-scattering detector (MiniDAWN TREOS; Wyatt Technology) and a refractive index detector (Optilab rEX; Wyatt Technology) on an ÄKTAmicro (GE Healthcare). An aliquot of 20 µl VP22_core (6 mg VP22_core ml⁻¹) was injected onto the pre-equilibrated column (20 mM HEPES, pH 7.5, 300 mM NaCl, 10 % glycerol and 2 mM TCEP) at a flow rate of 0.3 ml min⁻¹. astra 6 (Wyatt Technology) was used to determine the experimental protein molecular mass from the light-scattering data.

Hew K., Dahlroth S.L., Pan L.X., Cornvik T, & Nordlund P. (2015). VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies. The Journal of General Virology, 96(Pt 6), 1436-1445.

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Gel Filtration Analysis of SdrC Oligomerization

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To assess SdrC oligomerization, pure SdrC subdomains (1 mg ml⁻¹) were analyzed on a gel filtration column (Superdex 200 5/150 GL, GE Healthcare) attached to an AKTA FPLC at a flow rate of 0.3 ml min⁻¹ in TBS pH 7.4. The column was calibrated with the following proteins: thyroglobulin (660 KDa), ferritin (440 kDa), aldolase (158 kDa), conalbumin (75 kDa), ovalbumin (4 kDa), chymotrypsin (29 kDa), cytochrome c (12.4 kDa) and aprotinin (6.5 kDa) (Gel Filtration Calibration Kits HMW & LMW, GE Healthcare). Gel phase distribution coefficients (K_AV) were calculated from the respective elution volumes (Ve), represented as a function of molecular mass and analyzed by linear regression (R=0.9905). The relative molecular mass of SdrC species eluted from the column was calculated by interpolation.

Barbu E.M., Mackenzie C., Foster T.J, & Höök M. (2014). SdrC induces staphylococcal biofilm formation through a homophilic interaction. Molecular microbiology, 94(1), 172-185.

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Differential Scanning Calorimetry of Proteins

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To achieve identical buffer composition for reference and sample cells every sample was buffer exchanged using a Superdex‐200 5/150 GL or Superdex‐200 10/300 Increase column (GE Healthcare, Chicago, Illinois) connected to an HPLC 1260 Infinity with fraction collector (Agilent Technologies, Santa Clara, CA).
DSC experiments were performed with the PEAQ Differential Scanning Calorimeter Automated (Malvern Panalytical, Malvern, UK). Experiments were performed under increased pressure (~62 psi) to prevent the solutions from boiling. At the beginning of an experiment, at least four buffer runs (i.e., buffer in both sample and reference cells) were performed to establish the thermal history of the cells and to collect optimal buffer scans for buffer subtraction.
A temperature slope of 1°C/min was used for all experiments. Upon scanning from 20°C to 130°C and reheating again, we did not encounter any protein refolding. Therefore, the reheated run (i.e., rescan) was taken for buffer subtraction. Data analysis was performed with the PEAQ‐DSC analysis software (Malvern Panalytical, Malvern, UK). The baseline was fitted with the spline baseline correction model to account for differences in the heat capacities of the folded and unfolded states of the protein. Concentration normalization was performed and transitions were fitted with a two‐state thermal unfolding model.

Kotov V., Mlynek G., Vesper O., Pletzer M., Wald J., Teixeira‐Duarte C.M., Celia H., Garcia‐Alai M., Nussberger S., Buchanan S.K., Morais‐Cabral J.H., Loew C., Djinovic‐Carugo K, & Marlovits T.C. (2020). In‐depth interrogation of protein thermal unfolding data with MoltenProt. Protein Science : A Publication of the Protein Society, 30(1), 201-217.

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Recombinant Chimeric Antibody Purification

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Example 8

The expression and purification of the recombinant chimeric antibody protein produced above were conducted by following methods: HEK293E cells cultured in Freestyle 293 Expression Medium with 10% of Pluronic F-68 at 1×10⁶cell/ml were transfected with equal amount of heavy chain vector and light chain vector DNA with final concentration of 0.5 μg/ml and PEI (Polyethylenimine-linear, Polyscience) of 1.0 μg/ml. DNA to PEI ratio was 1:2. DNA and PEI complexes formed period with Optimal MEM should be 15 minutes at the room temperature. Transfected cells were cultured in the flasks with 5% CO₂, at 37° C. and at 125 rpm shaking speed. 1% Peptone medium was added at 22 to 26 hours post transfection. Conditioned medium was harvested on day 6 and supernatant was centrifuged at 3,000 rpm for 30 minutes. The clarified conditioned medium was then loaded onto ProteinA column (G.E. Healthcare), washed with PBS plus 0.1% triton-X100 and finally the bound IgG was eluted with a solution containing 0.1M glycine at pH 3.5. The eluted antibody protein was dialyzed to PBS and stored at −80° C. To remove endotoxin, the purified protein was further processed by passing through Hitrap DEAE Sepharose F.F. column and the resulting antibody was analyzed to determine the level of purity using size exclusion chromatography (Superdex 200 5/150 GL, G.E. Healthcare).

US10822416B2. Anti-PD-L1 antibodies (2020-11-03). MABSPACE BIOSCIENCES (SUZHOU) CO., LTD [CN]. Inventors: Xueming Qian [US], Teng Fei [CN], Zhen Li [CN].

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Recombinant Chimeric Antibody Production

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Example 8

US11753473B2. Anti-PD-L1 antibodies (2023-09-12). SUZHOU TRANSCENTA THERAPEUTICS CO., LTD. [CN]. Inventors: Xueming Qian [US], Teng Fei [CN], Zhen Li [CN].

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Structural Analysis of Scc2/4 Complexes

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Purified Scc2/4 was diluted in gel filtration buffer and adsorbed to glow discharged carbon-coated copper grids. After staining with 0.75% (wt/vol) uranyl formate, grids were imaged using a CM10 electron microscope (Philips, Amsterdam).
For size exclusion chromatography coupled to multiple angle light scattering (SEC-MALS), experiments were performed essentially as described previously (Hinshaw and Harrison, 2013 (link)) with the exception that a 3-ml size exclusion column was used for analysis of truncated Scc2^N–Scc4 complexes (Superdex 200 5/150 GL; GE Healthcare).

Hinshaw S.M., Makrantoni V., Kerr A., Marston A.L, & Harrison S.C. (2015). Structural evidence for Scc4-dependent localization of cohesin loading. eLife, 4, e06057.

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IstB ATPase Activity Assay

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IstB (32 µM) was incubated in the presence or absence of IstA (17 µM) in 40 µL of reaction buffer (50 mM HEPES pH 7.5, 300 mM NaCl, 10 mM MgCl₂, 10% glycerol, 1 mM β-mercaptoethanol), supplemented with either 1 mM ATP or ADP, for 30 min at 37 °C. Samples were subsequently run in over a Superdex 200 5/150 GL analytical gel filtration column (GE Healthcare), pre-equilibrated in reaction buffer.

Arias-Palomo E, & Berger J.M. (2015). An atypical AAA+ ATPase assembly controls efficient transposition through DNA remodeling and transposase recruitment. Cell, 162(4), 860-871.

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Protein Purification and Analytical Gel Filtration

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IstB, IstB_AAA+ and IstB active site mutants were dialyzed over-night at 4°C into 20 mM HEPES pH 7.5, 300 mM NaCl, 10 mM MgCl₂, 10% glycerol, 1 mM β-mercaptoethanol, with either 1 mM ATP or ADP. 40 µL at 1.5 mg/mL of each protein were then run over a Superdex 200 5/150 GL analytical gel filtration column (GE Healthcare) in the same buffer and monitored by A₂₈₀.

Arias-Palomo E, & Berger J.M. (2015). An atypical AAA+ ATPase assembly controls efficient transposition through DNA remodeling and transposase recruitment. Cell, 162(4), 860-871.

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Analytical Size-Exclusion Chromatography of rAPRc Isoforms

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Precursor rAPRc_99–231 and activated rAPRc_110–231 forms were analyzed under nondenaturing conditions by analytical size-exclusion chromatography on a Superdex 200 5/150 GL (GE Healthcare Life Sciences) column connected to a Prominence HPLC system (Shimadzu Corporation, Tokyo, Japan). The column was equilibrated in 20 mM phosphate buffer pH 7.5 containing 150 mM NaCl, and calibrated with Gel Filtration LMW and HMW calibration kits (GE Healthcare Life Sciences), according to the manufacturer's instructions. The molecular mass markers used for calibration were conalbumin (75 kDa), ovalbumin (43 kDa), carbonic anhydrase (29 kDa), and ribonuclease A (13.7 kDa).

Cruz R., Huesgen P., Riley S.P., Wlodawer A., Faro C., Overall C.M., Martinez J.J, & Simões I. (2014). RC1339/APRc from Rickettsia conorii Is a Novel Aspartic Protease with Properties of Retropepsin-Like Enzymes. PLoS Pathogens, 10(8), e1004324.

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