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Frac 950

Manufactured by GE Healthcare
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The Frac-950 is a laboratory instrument designed for high-performance liquid chromatography (HPLC) applications. It is capable of delivering precise and consistent mobile phase flow rates for analytical and preparative separation techniques.

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Lab products found in correlation

Unicorn 5, by GE Healthcare (2 mentions) Akta purifier system, by GE Healthcare (2 mentions) Superdex 75 10 300 gl, by GE Healthcare (1 mentions) Thyroglobulin, by GE Healthcare (1 mentions) Ferritin, by GE Healthcare (1 mentions) Aldolase, by GE Healthcare (1 mentions) Ovalbumin (ova), by GE Healthcare (1 mentions) Superose 6 increase 3.2 300 size exclusion chromatography column, by GE Healthcare (1 mentions) Akta fplc, by GE Healthcare (1 mentions) Unicorn software, by GE Healthcare (1 mentions) Phosphate buffered saline (pbs), by Capricorn (1 mentions) Superose 6 increase 10 300 gl column, by GE Healthcare (1 mentions) Ktapurifier 10, by GE Healthcare (1 mentions)

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Frac-950 fraction collector (4 citations) Frac 950 collector (2 citations)

8 protocols using frac 950

1

Knottin protein expression and purification

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The expression and
purification of EETI-II and mEETI-II knottins
was performed according to the protocol by Sankaran et al.13 (link) As an alternative to the dialysis purification,
size exclusion liquid chromatography (SEC) was performed using an
ÄKTA purifier with a Frac-950 fractionation collector (GE Healthcare
Life Sciences) (Figure S2C) equipped with
a Superdex 75 10/300GL (GE Healthcare Life Sciences) column. Both
methods gave comparable results. Concentrations of the knottins were
determined from the absorbance ε280nm = 5875 M–1 cm–1.
Klem R., de Ruiter M.V, & Cornelissen J.J. (2018). Protecting Encapsulin Nanoparticles with Cysteine-Knot Miniproteins. Molecular Pharmaceutics, 15(8), 2991-2996.
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2

Purification and Characterization of rCLCA1

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25 μg of affinity-purified rCLCA1 with C-terminal His was injected into a 2.2-ml Superose 6 Increase 3.2/300 size-exclusion chromatography column (GE Healthcare) with a size-exclusion range of 5000–3,000,000 Da using an EttanTM LC system (GE Healthcare) and the software Unicorn 5.01 (GE Healthcare). The system was run at a speed of 40 μl/min, eluting 1.5 column volumes of 50 mm HEPES, pH 7.4, 150 mm NaCl, collected in 100-μl fractions using a Frac950 (GE Healthcare) fraction collector and an ÄKTA BOX 900 (GE Healthcare). 5 mg/ml thyroglobulin (669,000 Da), ferritin (440,000 Da), aldolase (160,000 Da) and ovalbumin (42,700 Da) were used for column calibration and as molecular weight standards (GE Healthcare). The fractions containing rCLCA1 were determined through SDS-PAGE and Western blotting of all fractions showing a peak at 280-nm absorbance.
Nyström E.E., Arike L., Ehrencrona E., Hansson G.C, & Johansson M.E. (2019). Calcium-activated chloride channel regulator 1 (CLCA1) forms non-covalent oligomers in colonic mucus and has mucin 2–processing properties. The Journal of Biological Chemistry, 294(45), 17075-17089.
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3

Purification of OligoG-Polymyxin Conjugates

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OligoG–polymyxin conjugates were purified from the reaction mixture by fast protein liquid chromatography (FPLC) using an AKTA Purifier system (GE Healthcare; Amersham, UK) connected to a prepacked Superdex 75 16/600 GL column with a UV detector and a fraction collector (Frac-950). Data analysis was performed using Unicorn 5.31 software (2011; GE Healthcare; Amersham, UK). Samples (2 mL) were injected into a 2 mL loop using phosphate buffered saline (PBS) buffer (pH 7.4) as a mobile phase at 1 mL/min. Fractions were collected, pooled and lyophilised. Then, conjugates were re-dissolved in a minimal volume of dH2O and dialysed (1000 g/mol cut-off) against 5 × 1 L dH2O to remove PBS salts. The final conjugates were lyophilised and stored at −20 °C.
Stokniene J., Powell L.C., Aarstad O.A., Aachmann F.L., Rye P.D., Hill K.E., Thomas D.W, & Ferguson E.L. (2020). Bi-Functional Alginate Oligosaccharide–Polymyxin Conjugates for Improved Treatment of Multidrug-Resistant Gram-Negative Bacterial Infections. Pharmaceutics, 12(11), 1080.
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4

Molecular Weight Fractionation of BCP

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Materials PIB 39 -b-PEO36 BCP (M n 4.85 kg mol -1 ; polydispersity index 1.26) was supplied by BASF following a previously reported synthetic route. 44 Size exclusion chromatography (SEC) was chosen as the isolation technique for the different molecular weight (M w ) BCPs and was conducted with an Akta Explorer instrument (GE Life Sciences, Sweden). A semipreparative column (Tricorn 10/300, GE Life Sciences, Sweden) packed with Toyopearl HW-50F (Tosoh, Japan) served as the stationary phase and methanol was used as mobile phase. The sample concentration was set to 200 mg mL -1 and the flowrate of the mobile phase at 1 mL min -1 . Samples were injected manually using an INV-907 injection valve equipped with a 500 μl sample loop. The chromatograms were recorded with a UV-900 UV absorption detector operating at a wavelength of 280 nm. Fractions of 1 ml in volume were collected with a fraction collector (Frac-950, GE Life Sciences, Sweden). The solvent was removed from the fractions by evaporation.
Alvarez-Fernandez A., Reid B., Suthar J., Choy S.Y., Jara Fornerod M., Mac Fhionnlaoich N., Yang L., Schmidt-Hansberg B, & Guldin S. (2020). Fractionation of block copolymers for pore size control and reduced dispersity in mesoporous inorganic thin films. Nanoscale, 12(35).
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5

Purification of Papain-Digested Proteins

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The purification of proteins/peptides present in the papain digests was done by utilizing the Fast Protein Liquid Chromatography [ÄKTA purifier Frac-950] using a size exclusion chromatography column (GE XK16, 16×100 mm) and superdex G-30 matrix with a separation range of MW 0.5–10 kDa. The matrix was packed into the column and equilibrated with phosphate buffer (0.05 M; pH 6.9) over 5 column volumes. After equilibration, 30 milligrams of double filtered (0.22 μm syringe filter) papain hydrolysate was loaded into the column. The different fractions were eluted out of the column at a specific flow rate (0.5 ml/min). Fractions were pooled together based on the protein and peptide maxima detected at 280 nm and 215 nm respectively and directly lyophilized and stored at -20°C.
Pachaiappan R., Tamboli E., Acharya A., Su C.H., Gopinath S.C., Chen Y, & Velusamy P. (2018). Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. PLoS ONE, 13(3), e0193717.
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6

Purification of Human IgG Antibodies

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Total IgG purification and affinity purification of antibodies were performed by FPLC (AKTA FPLC with Frac-950 and Unicorn Software; GE Healthcare). Human plasmapheresis fluid was obtained from the UNC-Chapel Hill apheresis facility following approval by the IRB and informed patient consent. Total IgG was purified by precipitation of total serum proteins with 50% ammonium sulfate, resuspensded into approximately 20 mL PBS, and dialyzed into PBS over 72 hrs with three successive dialysate switches.
Reynolds J., Preston G.A., Pressler B.M., Hewins P., Brown M., Roth A., Alderman E., Bunch D., Jennette J.C., Cook H.T., Falk R.J, & Pusey C.D. (2015). Autoimmunity to the alpha 3 chain of type IV collagen in glomerulonephritis is triggered by ‘autoantigen complementarity’. Journal of autoimmunity, 59, 8-18.
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7

EV Isolation via Size-exclusion Chromatography

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PL was centrifuged at 1500× g for 15 min at 4 °C. The supernatant was filtered through 0.8 µm porous membrane (Sartorius) for large cell debris elimination and then through 0.2 µm porous membrane (Sartorius). PL was centrifuged at 10,000× g for 30 min at 4 °C to preferentially retain small EVs. The supernatant (5 mL) was loaded on a Sepharose CL−2B precast column (GE Healthcare, Pittsburg, PA, USA). AKTA purifier system coupled with a collector Frac 950 (GE Healthcare) was used to set a flow rate at 0.5 mL/min. EVs were eluted with PBS (Capricorn, Ebsdorfergrund, Germany) in 5 mL fractions, which were collected and characterized (Supplementary Figure S1). The ninth fraction was used for the experiments since it presented strong bands for the specific CD9 Western blot marker while preserving low levels of protein concentration.
Antich-Rosselló M., Munar-Bestard M., Forteza-Genestra M.A., Calvo J., Gayà A., Monjo M, & Ramis J.M. (2022). Evaluation of Platelet-Derived Extracellular Vesicles in Gingival Fibroblasts and Keratinocytes for Periodontal Applications. International Journal of Molecular Sciences, 23(14), 7668.
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8

Serum HDL Separation by Size-Exclusion Chromatography

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The serum HDL separation was performed by size-exclusion chromatography (SEC) using a previously described method [67 (link)]. Briefly, fractions were determined in 50 μL of serum samples diluted with 50 μL of a PBS solution via SEC, using a Superose 6 increase column (10/300GL, 10 × 300, 24 mL), (GE Healthcare; Uppsala, Sweden). SEC was carried out using an ÄKTA purifier 10 (GE Healthcare; Uppsala, Sweden), equipped with a fraction collector (Frac-950). The system was controlled by a UNICORN control system, version 4.10 (GE Healthcare; Uppsala, Sweden). The SEC flow rate was set at 450 μL/min. Eluting fractions were collected in glass-coated 96-well plates (Eppendorf Protein Low-Bind; Hamburg, Germany). The HDL fractions were combined after fractionation, and samples were dried in a vacuum centrifuge and stored at −80 °C before further processing. Lipids from the selected fractions obtained by Superose-6 SEC were further extracted and investigated by LC-MS, as detailed below.
Mocciaro G., D’Amore S., Jenkins B., Kay R., Murgia A., Herrera-Marcos L.V., Neun S., Sowton A.P., Hall Z., Palma-Duran S.A., Palasciano G., Reimann F., Murray A., Suppressa P., Sabbà C., Moschetta A., Koulman A., Griffin J.L, & Vacca M. (2022). Lipidomic Approaches to Study HDL Metabolism in Patients with Central Obesity Diagnosed with Metabolic Syndrome. International Journal of Molecular Sciences, 23(12), 6786.
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