Biflex 4

Manufactured by Bruker

Sourced in Germany

The Biflex IV is a mass spectrometer that utilizes matrix-assisted laser desorption/ionization (MALDI) technology for the analysis of biomolecules. It is designed to provide high-resolution and accurate mass measurement capabilities for a wide range of applications.

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Lab products found in correlation

C18 ziptip, by Merck Group (2 mentions) Speedvac, by Thermo Fisher Scientific (1 mentions) 1200 hplc, by Agilent Technologies (1 mentions) Nmr spectrometer, by Agilent Technologies (1 mentions) Avance 2 nmr spectrometer, by Bruker (1 mentions) Ft ir 4100, by Jasco (1 mentions) Combiflash system, by Teledyne (1 mentions) P 2000, by Jasco (1 mentions) V 630 spectrometer, by Jasco (1 mentions) Uv 2075, by Jasco (1 mentions) 6230 tofms, by Agilent Technologies (1 mentions) Mx 2080 32, by Jasco (1 mentions)

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Biflex IV MALDI-TOF MS (4 citations)

4 protocols using biflex 4

Protein Spot Identification by MALDI-TOF MS

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All of the protein spots of interest were manually excised. The gel pieces were destained in 60% acetonitrile in 25 mM ammonium bicarbonate buffer, pH 8.5, and dehydrated with 100% acetonitrile. The shrunken gel pieces were re-swollen in 25 mM ammonium bicarbonate buffer, dehydrated again in 100% acetonitrile, and dried in a SpeedVac (Thermo Scientific, Milford, MA, USA). The gel pieces were re-hydrated in 10 μL trypsin solution (20 μg/mL) for 1 h, followed by addition of 5 μL 25 mM ammonium bicarbonate buffer to completely immerse the gel pieces. After incubation overnight at 37 °C, 0.5 μL incubation buffer was mixed with 0.5 μL matrix solution (CHCA 2 mg/mL in 50% acetonitrile and 1% TFA) and pipetted directly onto the stainless steel sample plate of the mass spectrometer. The samples were analyzed by MALDI-TOF MS (Biflex IV, Bruker Daltonics, Bremen, Germany). In cases where the MS signals were weak, the peptides were enriched by C18 ZipTip (Millipore, Billerica, MA, USA) according to the manufacturer’s instructions. The bound peptides were eluted from the ZipTip using 1 μL CHCA, which was directly deposited onto the metal plate.

Ma H.I., Hueng D.Y., Shui H.A., Han J.M., Wang C.H., Lai Y.H., Cheng S.Y., Xiao X., Chen M.T, & Yang Y.P. (2014). Intratumoral Decorin Gene Delivery by AAV Vector Inhibits Brain Glioblastomas and Prolongs Survival of Animals by Inducing Cell Differentiation. International Journal of Molecular Sciences, 15(3), 4393-4414.

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Characterization of Organic Compounds

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Optical rotations were measured on a JASCO P-2000 at the D-double emission line of Na°. UV-vis spectra were measured on a JASCO V-630 spectrometer. FTIR spectra were collected on thin-film samples using a JASCO FTIR-4100 fitted with an ATR accessory (ZnSe plate). 1D NMR and inverse-detected 2D NMR spectra were measured on a Bruker Avance II NMR spectrometer with a 1.7 mm¹H{¹³C/¹⁵N} 600 MHz microcryoprobe. Other NMR spectra were measured on a JEOL ECA spectrometer equipped with a 5 mm¹H{¹³C} 500 MHz room-temperature probe.¹³C NMR spectra were measured using a Varian NMR spectrometer equipped with a 5 mm Xsens¹³C{¹H} 125 MHz cryoprobe. NMR spectra are referenced to residual solvent signals. High-resolution ESITOF analysis was carried out on an Agilent 1200 HPLC coupled to an Agilent 6230 TOFMS. Low-resolution MALDI MS measurements were made on a Bruker Biflex IV in a nitrobenzyl alcohol matrix. Low-resolution MS measurements were made on a Thermoelectron Accela UHPLC coupled to an MSQ single-quadrupole detector. Preparative, semipreparative, and analytical HPLC were performed on a JASCO PU-2086 Plus system consisting of a dynamic mixer (MX-2080–32) with UV-VIS detector (UV-2075) operating at λ 250 nm. Automated flash chromatography was carried out with a Teledyne-Isco CombiFlash system with UV (λ 250 nm) and RI detection.

Gartshore C.J., Salib M.N., Renshaw A.A, & Molinski T.F. (2017). Isolation of Bastadin-6-O-Sulfate and Expedient Purifications of Bastadins-4, −5 and −6 from Extracts of Ianthella basta. Fitoterapia, 126, 16-21.

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MALDI-TOF Analysis of Triphosphorylated Substrate

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Substrate RNAs were prepared as described for the trans-triphosphorylation reaction, but without internal radiolabeling. A fraction of the substrate was incubated with an excess of the TPR1 ribozyme for 3 h. The product of the triphosphorylation reaction and unreacted substrate RNA were purified by denaturing PAGE, and desalted on C₁₈ Zip-tips (Millipore). About 20 pmol of each sample were dissolved in 4 µl containing 3-hydroxypicolinic acid and diammonium hydrogen citrate, and spotted on matrix-assisted laser desorption/ionization (MALDI) targets. The mass spectra were recorded by Dr Yongxuan Su at the UCSD Molecular Mass Spectrometry Facility in negative ion mode on a Bruker Biflex IV, MALDI-time-of-flight mass spectroscopy (TOFMS).

Moretti J.E, & Müller U.F. (2014). A ribozyme that triphosphorylates RNA 5′-hydroxyl groups. Nucleic Acids Research, 42(7), 4767-4778.

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Mass Spectrometry-based Protein Identification

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Each differentially expressed spot from the gels was dehydrated with 50 ml of ACN for 5 min, incubated in 50 mL of 10 mM DTT at 56 uC for 1 hour, and then incubated in 50 mL of 55 mM iodoacetamide (alkylating solution) for 45 min. The spots were dehydrated with 50 ml of ACN and rehydrated in 5 ml of porcine trypsin, followed by the addition of 10 ml of 25 mM ammonium bicarbonate. Proteolysis was performed overnight at 37 uC and stopped by adding 10 ml of 2% formic acid. Resulting peptides were concentrated and mixed with alpha-cyano-4-hydroxycinam-mic acid (Sigma, St. Louis, MO, USA), deposited on a 384-well MALDI target, and air-dried. Analyses were performed with a Biflex IV (Bruker Daltonics, Germany). MS data were compared against tryptic peptide sequences from the SWISS-PROT database using Mascot (Matrix Sciences, London, UK) search algorithms.

Liu H., Cheng Z., Song W., Wu W, & Zhou Z. (2014). Immunoproteomic to Analysis the Pathogenicity Factors in Leukopenia Caused by Klebsiella Pneumonia Bacteremia. PLoS ONE, 9(10), e110011.

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