P ace mdq

Manufactured by Beckman Coulter

Sourced in United States

The P/ACE MDQ is a capillary electrophoresis system designed for the separation and analysis of a variety of biomolecules, including proteins, nucleic acids, and small molecules. It provides high-resolution separation and sensitive detection capabilities for applications in the life sciences and analytical chemistry fields.

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Lab products found in correlation

P ace 5000, by Beckman Coulter (5 mentions) Fused silica capillary, by Molex (2 mentions) Nanodrop 2000 2000c, by Thermo Fisher Scientific (1 mentions) Jem 1010, by JEOL (1 mentions) Pd 10 desalting column, by Cytiva (1 mentions) Hplc grade water, by Carl Roth (1 mentions) Microtof ms, by Bruker (1 mentions) Cation analysis kit, by AB Sciex (1 mentions) Jupiter c18 column, by Phenomenex (1 mentions) Rat albumin elisa quantitation kit, by Fortis Life Sciences (1 mentions) 0.2 μm membrane filter, by Merck Group (1 mentions) Fused silica capillaries, by Molex (1 mentions) 32 karat software, by Beckman Coulter (1 mentions) Uncoated fused silica capillary, by Molex (1 mentions) Milli q, by Merck Group (1 mentions) 2002 potentiometer, by Crison (1 mentions) Fused silica capillaries, by Agilent Technologies (1 mentions) Pseudomonas isoamylase, by Megazyme (1 mentions)

Close spelling variants of this product

P/ACETM MDQ electrophoresis system P/ACETM MDQ system P/ACETM MDQ P/ACE MDQ Carbohydrate System Beckman P/ACE MDQ system P/ACE MDQ Glycoprotein System P/ACE MDQ CE instrument Beckman P/ACE MDQ capillary electrophoresis system P/ACE MDQ CE system Beckman P/ACE™ MDQ

35 protocols using p ace mdq

Preparation and Characterization of PA6-NFsM

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The CE instrument (P/ACE MDQ, Beckman, Brea, CA, USA) was equipped with a diode array detector, and a chromatographic workstation. An electrostatic spinning machine (Yongkang Leye, Beijing, China) was used to prepare PA6-NFsM. A scanning electron microscope (SEM, S-4800I, Hitachi, Japan) and Fourier transform infrared spectrometer (Nicolet iS, Thermo Fisher, Waltham, MA, USA) were employed to characterize PA6 and PA6-PPy-NFsM.

Li X., Miao J., Yin Z., Xu X, & Shi H. (2019). Polypyrrole-Modified Nylon 6 Nanofibers as Adsorbent for the Extraction of Two β-Lactam Antibiotics in Water Followed by Determination with Capillary Electrophoresis. Molecules, 24(12), 2198.

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Carbohydrate Derivatization and CZE Analysis

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The carbohydrates for CZE electrophoresis were derivatized as described by Noe and Freissmuth [100 (link)]. CZE equipment: Beckman Coulter P/ACE MDQ (Beckman Coulter, Brea, USA); fused silica capillary, 70/77 cm × 50 μm i.d.; running buffer, 50 mM Na₂B₂O₇ pH 10.3, MeCN 4.4 mol/L added; injection, 5−10 s at 0.5 psi; voltage, 30 kV; detection, λ = 200 nm; software, 32 Karat software version 5.0 (Beckman Coulter).

, & Spiegler V. (2020). Anthelmintic A-Type Procyanidins and Further Characterization of the Phenolic Composition of a Root Extract from Paullinia pinnata. Molecules, 25(10), 2287.

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Analyzing Oligomeric Compounds in 96-Well Plates

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Example 5

Analysis of Oligomeric Compounds Using the 96-Well Plate Format

The concentration of oligomeric compounds in each well can be assessed by dilution of samples and UV absorption spectroscopy. The full-length integrity of the individual products can be evaluated by capillary electrophoresis (CE) in either the 96-well format (Beckman P/ACE™ MDQ) or, for individually prepared samples, on a commercial CE apparatus (e.g., Beckman P/ACE™ 5000, ABI 270). Base and backbone composition is confirmed by mass analysis of the oligomeric compounds utilizing electrospray-mass spectroscopy. All assay test plates are diluted from the master plate using single and multi-channel robotic pipettors. Plates are judged to be acceptable if at least 85% of the oligomeric compounds on the plate are at least 85% full length.

US11180756B2. Morpholino modified oligomeric compounds (2021-11-23). Ionis Pharmaceuticals, Inc. [US]. Inventors: Michael Oestergaard [US], Punit P. Seth [US].

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Characterization of Saponin-Containing Samples

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CE evaluation were carried out on a Beckman Coulter P/ACE MDQ instrument with UV detector (Fullerton, CA, USA). The wavelength for UV detection was set at 260 nm for ssDNA and 203 nm for saponins. PCR amplification was implemented on an ABI GeneAmp 9700 instrument (Shanghai, China). Transmission electron microscopy (TEM) characterization was carried out on a JEOL JEM-1010 instrument (Tokyo, Japan). The ultraviolet (UV) spectra were recorded by a Thermo Fisher NanoDrop 2000/2000C spectrophotometer (MA, USA).

Zhang H., Li X., Huang A., Yan Z., Chen Y, & Bie Z. (2021). PEI-assisted boronate affinity magnetic nanoparticle-based SELEX for efficient in vitro evolution of saponin-binding aptamers. RSC Advances, 11(15), 8775-8781.

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Sulfate Turnover Determination in Peat Soils

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Sulfate and substrate concentrations at days 0, 4, 7, 11, 14, 18, 21, 25, 28, 35, 42, and 49 were determined by capillary electrophoresis (P/ACE MDQ, Beckman Coulter, Brea, CA, USA) directly after amendment using the CEofix anions 5 kit (Analis, Suarlée, Belgium). To obtain substrate-specific sulfate turnover rates, we determined how much sulfate was utilized in the substrate- and sulfate-amended microcosms in comparison to the sulfate-amended controls without external substrate. This served to discriminate against sulfate dissimilation caused by SRMs using endogenous substrates and sulfate assimilation in general. The calculation was performed by subtracting average sulfate concentrations of the sulfate-amended no-substrate controls from the individual substrate- and sulfate-amended microcosms at each corresponding time point. A nonparametric regression was fitted to the obtained values in R (R Core Team, 2015 ), and the slope of the regression curve was used to calculate net sulfate turnover rates (ST). Sulfate concentrations were previously converted from μM to nmol per cm³ of fresh peat soil using the measured soil water content (78%, Supplementary Methods) and the bulk density of peat soil (0.29 g cm⁻³; Goldberg et al., 2008 (link)) to allow comparison with results obtained in other studies (for example, Knorr et al., 2009 ; Knorr and Blodau, 2009 ).

Hausmann B., Knorr K.H., Schreck K., Tringe S.G., Glavina del Rio T., Loy A, & Pester M. (2016). Consortia of low-abundance bacteria drive sulfate reduction-dependent degradation of fermentation products in peat soil microcosms. The ISME Journal, 10(10), 2365-2375.

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Cerebrospinal Fluid Sampling and Analysis

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Cerebrospinal fluid sample collection and its analysis was performed as described previously in (9 (link)). Briefly, CSF was centrifuged immediately after collection (1600 g, 4 °C, 15 minutes), aliquoted into polypropylene test tubes (each aliquot, 750 µL), frozen within 30–40 minutes after the puncture and stored at −80 C until use. After thawing, 700 µL of CSF were diluted with 700 µL buffer (pH 10.5; 2 M urea, 100 mmol/L NaCl, 0.0125% NH₃) and ultracentrifuged using Centrisart ultrafiltration devices (cut off 20 kDa) at 4 °C until 1.1 mL of filtrate was obtained. Subsequently the filtrate was applied onto a PD-10 desalting column (Amersham Biosciences, Freiburg, Germany) equilibrated in 0.01% NH₄OH in HPLC-grade water (Roth, Karlsruhe, Germany), and the eluate was lyophilized, stored at 4 °C and resuspended in 10 µL HPLC-grade water before capillary electrophoresis–mass spectrometry (CE-MS) analysis. CE-MS analysis was performed as described using a P/ACE MDQ (Beckman Coulter, Krefeld, Germany) system on-line coupled to a Micro-TOF MS (Bruker Daltonic, Bremen, Germany) (9 (link), 22–24 (link)).

Barrera-Ocampo A., Arlt S., Matschke J., Hartmann U., Puig B., Ferrer I., Zürbig P., Glatzel M., Sepulveda-Falla D, & Jahn H. (2016). Amyloid-β Precursor Protein Modulates the Sorting of Testican-1 and Contributes to Its Accumulation in Brain Tissue and Cerebrospinal Fluid from Patients with Alzheimer Disease. Journal of Neuropathology and Experimental Neurology, 75(9), 903-916.

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Oligomeric Compound Quality Analysis

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Example 5

Analysis of Oligomeric Compounds Using the 96-Well Plate Format

US10344275B2. Linkage modified oligomeric compounds (2019-07-09). Ionis Pharmaceuticals, Inc. [US]. Inventors: W. Brad Wan [US], Michael T. Migawa [US], Michael Oestergaard [US], Eric E. Swayze [US], Punit P. Seth [US].

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Capillary Electrophoresis Analysis of Cell Extracts

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The 100 μL cell suspension, as indicated above, in an amber microcentrifuge tube was mixed with 0.1% MPA in a 1:2 volumetric ratio, and then it was centrifuged at 12,000 × g for 10 minutes after being adequately mixed by a vortex mixer. The supernatant was assayed on a capillary electrophoresis analyzer (P/ACE MDQ, Beckman Coulter) after being filtered with a 0.2 μm syringe set. The analysis was performed at a constant temperature (28 °C) with 300 mM borate running buffer (pH 7.8) and a UV absorbance detector set to 200 nm.

Cheng S.H., Tseng Y.M., Wu S.H., Tsai S.M, & Tsai L.Y. (2017). Whey Protein Concentrate Renders MDA-MB-231 Cells Sensitive to Rapamycin by Altering Cellular Redox State and Activating GSK3β/mTOR Signaling. Scientific Reports, 7, 15976.

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Capillary Electrophoresis for Ammonium Analysis

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For determination of ammonium, capillary electrophoresis (P/ACE MDQ, Beckman & Coulter) was employed, which is known to constitute a highly efficient and effective separation method for analysis of ionic species in general and thus also ammonium in particular [12 (link)–15 (link)]. The capillary was made of fused silica and had an effective length of 50 cm with an inner diameter of 75 µm and outer diameter of 375 µm. The samples were diluted 50-fold with ultrapure water. If no ammonium could be detected using this dilution factor, measurement was repeated with a 10-fold dilution. The volume was injected into the capillary using pressure injection, and separation took place at 30 kV with normal capillary polarity. Measurements were executed using a Cation Analysis Kit (ABSciex, Darmstadt, Germany). Indirect detection was performed with the help of a diode array analyzer at 200 nm. The temperature of tray and capillary was set to 25°C. The measurements were performed by one person only who underwent a detailed initial training program previously.
The absolute amounts of ammonium were calculated by taking the total urine volume of which the sample was taken into consideration.

Roehrborn F., Dohle D.S., Waack I.N., Tsagakis K., Jakob H, & Teloh J.K. (2017). Postoperative Compensatory Ammonium Excretion Subsequent to Systemic Acidosis in Cardiac Patients. BioMed Research International, 2017, 5383574.

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Histone Acetylation Profiling by HPLC and HPCE

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Histone acid extraction (sulfuric acid + acetone precipitation) and global histone acetylation was performed as previously described (41 (link),42 (link)) with slight modifications. In brief, individual fractions of histones H4, H3, H2A and H2B were purified by reversed-phase high-performance liquid chromatography (HPLC) on a Jupiter C18 column (Phenomenex, Inc.) and eluted with an acetonitrile gradient (20–60%) in 0.3% trifluoroacetic acid using an HPLC gradient system (Beckman Coulter). Acetylated histone derivatives were resolved by high-performance capillary electrophoresis (HPCE) using an uncoated fused-silica capillary tubing (Beckman-Coulter; 60.2 cm × 75 μm, effective length 50 cm) in a capillary electrophoresis system (P/ACE MDQ, Beckman-Coulter) with 100 mM phosphate buffer (pH 2.0) 0.02% (w/v) HPM-cellulose as running buffer and an operating voltage of 12 kV.

Urdinguio R.G., Lopez V., Bayón G.F., Diaz de la Guardia R., Sierra M.I., García-Toraño E., Perez R.F., García M.G., Carella A., Pruneda P.C., Prieto C., Dmitrijeva M., Santamarina P., Belmonte T., Mangas C., Diaconu E., Ferrero C., Tejedor J.R., Fernandez-Morera J.L., Bravo C., Bueno C., Sanjuan-Pla A., Rodriguez R.M., Suarez-Alvarez B., López-Larrea C., Bernal T., Colado E., Balbín M., García-Suarez O., Chiara M.D., Sáenz-de-Santa-María I., Rodríguez F., Pando-Sandoval A., Rodrigo L., Santos L., Salas A., Vallejo-Díaz J., C. Carrera A., Rico D., Hernández-López I., Vayá A., Ricart J.M., Seto E., Sima-Teruel N., Vaquero A., Valledor L., Cañal M.J., Pisano D., Graña-Castro O., Thomas T., Voss A.K., Menéndez P., Villar-Garea A., Deutzmann R., Fernandez A.F, & Fraga M.F. (2019). Chromatin regulation by Histone H4 acetylation at Lysine 16 during cell death and differentiation in the myeloid compartment. Nucleic Acids Research, 47(10), 5016-5037.

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