P ace mdq glycoprotein system

Manufactured by Beckman Coulter

Sourced in United States

The P/ACE MDQ Glycoprotein System is a capillary electrophoresis instrument designed for the analysis of glycoproteins. It utilizes capillary zone electrophoresis technology to separate and detect glycoproteins in a sample.

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P/ACE MDQ (35 citations) P/ACE (7 citations)

3 protocols using p ace mdq glycoprotein system

Cloning and Purification of OsUGE-1 Epimerase

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The coding sequence of the OsUGE-1 was amplified using PCR and cloned into the pET-15b plasmid vector (Novagen). The resulting plasmid was transformed into E. coli BL21 (DE3) and grown in LB medium, and IPTG (isopropyl-1-thio-β-D-galactopyranoside) was used to induce the expression of the recombinant protein [22] . The enzyme was purified from the cell lysate using a Ni²⁺-NTA affinity column that binds to the epimerase’s N-terminal hexahistidine sequence [22] . The enzyme activity assays were performed as outlined in Chen et al. (1999)[22] . Briefly, OsUGE1 activity was assayed in a 200 µL reaction mixture containing 20 mM Tris/HCl (pH 8.0), 1 mM NAD⁺, and 1 mM UDP-gal or UDP-glc, and incubated at 37°C for 30 minutes, and quickly terminated by transferring the reaction tube to 100°C for 5 minutes. The UDP-gal or UDP-glc products were quantified using capillary electrophoresis using a P/ACE MDQ Glycoprotein System (Beckman Coulter) with UV detection, according to Westman et al. (2006)[23] (link).

Guevara D.R., El-Kereamy A., Yaish M.W., Mei-Bi Y, & Rothstein S.J. (2014). Functional Characterization of the Rice UDP-glucose 4-epimerase 1, OsUGE1: A Potential Role in Cell Wall Carbohydrate Partitioning during Limiting Nitrogen Conditions. PLoS ONE, 9(5), e96158.

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Capillary Electrophoresis of Amyloid-Beta Oligomers

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Aliquots of 15 μL were separated via CE in 0.5% w/v polyethylene oxide (PEO; 2 MDa, Sigma-Aldrich, St. Louis, MO) coated capillaries (L_t = 31 cm; L_d = 10 cm) with a 0.5% PEO (300 kDa, Sigma-Aldrich) separation matrix and a capillary temperature of 25°C. Capillaries were dynamically coated by rinsing with water (10 min at 20 psi), 0.1 M HCl (15 min at 20 psi), 0.5% PEO (2 MDa) in water (20 min at 50 psi), and with water (15 min at 20 psi). CE separations using UV detection (214 nm) were performed using a P/ACE MDQ Glycoprotein System from Beckman Coulter, (Fullerton, CA). Samples were pressure injected at 0.5 psi for 8 s and separated at 7 kV. Between each run, the capillary was rinsed with deionized water for 10 min.
To correlate electrophoresis peaks with approximate molecular weights, 50 μL aliquots of aggregated Aβ_1–40 were removed at selected times and ultrafiltrated (20 min, 14,100 × g) through Amicon (Millipore, Billerica, MA) filters with molecular weight cutoff values of 10, 30, 50, 100, and 300 kDa. The filtrate and retentate were analyzed via UV-CE to verify elution times for oligomers within each molecular weight range.

Pryor N.E., Moss M.A, & Hestekin C.N. (2014). Capillary electrophoresis for the analysis of the effect of sample preparation on early stages of Aβ1–40 aggregation. Electrophoresis, 35(0), 1814-1820.

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Capillary Electrophoresis of Glycoproteins

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CE analyses were carried out according to Bao et al. [20] . A P/ACE MDQ Glycoprotein System (Beckman Coulter, Brea, CA, USA), with an uncoated capillary (ID = 50 µm; effective length = 50 cm; Beckman Coulter, Brea, CA, USA) was used.
The run buffer solution was 55% aqueous (200 mM NaH2PO4, pH 7.05, containing 100 mM SDS) and 45% methanol. Sample injection was performed by pressure at 0.7 psi for 6 s and electrophoretic conditions were positive to negative (+30 kV) at 25°C. Detection wavelength was 200 nm.

Monti L., Cattaneo T.M., Orlandi M, & Curadi M.C. (2015). Capillary electrophoresis of sialylated oligosaccharides in milk from different species. Journal of chromatography. A, 1409.

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