Akta purifier chromatography system

Manufactured by GE Healthcare

Sourced in United Kingdom

The AKTA Purifier is a chromatography system designed for the purification of biomolecules, such as proteins, peptides, and other macromolecules. It is a versatile and automated system that can perform various separation techniques, including ion exchange, size exclusion, and affinity chromatography. The AKTA Purifier is equipped with advanced features, such as precise flow control, accurate UV and conductivity detection, and intuitive software for method development and data analysis.

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Lab products found in correlation

Hitrap q hp 5 ml column, by GE Healthcare (2 mentions) Nanodrop 2000c spectrophotometer, by Thermo Fisher Scientific (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) 30k mwco, by Merck Group (1 mentions) Chromatography column, by Bio-Rad (1 mentions) Protein g agarose, by Roche (1 mentions) Sephadex g 25 fine, by GE Healthcare (1 mentions)

4 protocols using akta purifier chromatography system

Purification of IRDIG35563 Protein

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Example 4

IRDIG35563 Purification.

Harvested Pf cells containing IRDIG35563 were sonicated in lysis buffer consisting of 50 mM Tris (pH 8.0), 1 M NaCl, 10% glycerol and 2 mM EDTA with 50 μL of Protease Inhibitor Cocktail (Sigma-Aldrich, St. Louis, Mo.) per 25 mL buffer. The extract was centrifuged at 20,000×g for 40 minutes. The soluble protein in the supernatant was precipitated with 50% ammonium sulfate and centrifuged at 20,000×g for 30 minutes. The pellet was resuspended in 50 mM Tris (pH 8.0) and centrifuged at 20,000×g for 20 minutes to pellet any soluble material. The supernatant containing IRDIG35563 was purified by anion exchange chromatography using a HiTrap™ Q HP 5 mL column with an AKTA Purifier chromatography system (GE Healthcare, UK). The column was equilibrated in 50 mM Tris (pH 8.0), and proteins were eluted with a stepwise gradient to 1 M NaCl. Protein-containing fractions were combined and concentrated using Amicon® Ultra-15 Centrifugal Filter Devices with a 30K MWCO (EMD Millipore, Burlington, Mass.). The IRDIG35563 protein sample was dialyzed overnight against 50 mM Tris (pH 8.), and total protein concentrations were measured with the NanoDrop 2000C Spectrophotometer (Thermo Scientific, Waltham, Mass.), using the A280 method.

US11274315B2. Chimeric insecticidal proteins (2022-03-15). CORTEVA AGRISCIENCE LLC [US]. Inventors: Marc D Zack [US], Megan Sopko [US], James M Hasler [US].

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Purification of HIT IgG from Patient Plasma

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Total HIT IgG was purified from patients’ plasma with Protein G Agarose (Roche Mannheim, Germany). Resin (2 ml for 10 ml of plasma) was packed into a chromatography column (1.5 cm × 10 cm; Bio-Rad, Hercules, CA, USA), and the purification procedure was conducted with AKTA purifier chromatography system (GE Healthcare). The eluted peak fractions were pooled and concentrated using ultracentrifugal unit (10 kDa) (Millipore, Billerica, MA, USA). Activity of purified HIT IgG was determined by platelet aggregation and serotonin release assays.

Perdomo J., Leung H.H., Ahmadi Z., Yan F., Chong J.J., Passam F.H, & Chong B.H. (2019). Neutrophil activation and NETosis are the major drivers of thrombosis in heparin-induced thrombocytopenia. Nature Communications, 10, 1322.

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Reduction and Purification of 3'Thiol-DV230

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A solution of 3′disulfide-DV230
at 25 ± 2.5 mg/mL in 100 mM sodium phosphate, 150 mM sodium chloride,
1 mM ethylenediaminetetraacetic acid (EDTA), pH 7.5 was reduced by
the addition of 5 equiv of tris(2-carboxyethyl)phosphine hydrochloride
(TCEP, Thermo Scientific, Rockford, IL) for 2 h at 40 ± 2 °C.
The 3′thiol-DV230 oligonucleotide was isolated by gel filtration
(desalting) using Sephadex G-25 Fine, GE Healthcare, Pittsburgh, PA,
packed into XK50/30 columns, according to the manufacturer’s
recommended procedures and controlled by an AKTA purifier chromatography
system (GE Healthcare, Pittsburgh, PA). The 3′thiol-DV230 was
loaded onto a G25 column equilibrated with 100 mM NaPO4, 150 mM NaCl,
1 mM EDTA, pH 7.5 at a flow rate of 30 cm/h in a volume of ∼12–16%
of the packed column volume. The 3′thiol-DV230 was collected
starting when the UV signal (A215 nm) rose above ∼100 mAU and
ending when a pool volume of 1.6 to 1.8 times the load volume was
collected. The G25 purified 3′thiol-DV230 was stored frozen
at −80 °C.

Milley B., Kiwan R., Ott G.S., Calacsan C., Kachura M., Campbell J.D., Kanzler H, & Coffman R.L. (2016). Optimization, Production, and Characterization of a CpG-Oligonucleotide-Ficoll Conjugate Nanoparticle Adjuvant for Enhanced Immunogenicity of Anthrax Protective Antigen. Bioconjugate Chemistry, 27(5), 1293-1304.

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IRDIG35563 Protein Purification

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Example 4

IRDIG35563 purification. Harvested Pf cells containing IRDIG35563 were sonicated in lysis buffer consisting of 50 mM Tris (pH 8.0), 1 M NaCl, 10% glycerol and 2 mM EDTA with 50 μL of Protease Inhibitor Cocktail (Sigma-Aldrich, St. Louis, Mo.) per 25 mL buffer. The extract was centrifuged at 20,000×g for 40 minutes. The soluble protein in the supernatant was precipitated with 50% ammonium sulfate and centrifuged at 20,000×g for 30 minutes. The pellet was resuspended in 50 mM Tris (pH 8.0) and centrifuged at 20,000×g for 20 minutes to pellet any soluble material. The supernatant containing IRDIG35563 was purified by anion exchange chromatography using a HiTrap™ Q HP 5 mL column with an AKTA Purifier chromatography system (GE Healthcare, UK). The column was equilibrated in 50 mM Tris (pH 8.0), and proteins were eluted with a stepwise gradient to 1 M NaCl. Protein-containing fractions were combined and concentrated using Amicon® Ultra-15 Centrifugal Filter Devices with a 30K MWCO (EMD Millipore, Burlington, Mass.). The IRDIG35563 protein sample was dialyzed overnight against 50 mM Tris (pH 8.), and total protein concentrations were measured with the NanoDrop 2000C Spectrophotometer (Thermo Scientific, Waltham, Mass.), using the A280 method.

US11781152B2. Chimeric insecticidal proteins (2023-10-10). CORTEVA AGRISCIENCE LLC [US]. Inventors: Marc D Zack [US], Megan Sopko [US], James M Hasler [US].

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