N-terminal rhodamine, FITC and Cy5-labeled Bim BH3 peptides were synthesized on Rink Amide-MBHA resin using Fmoc synthesis and DIC/HOBt coupling with an Advanced Chem Tech 396 multiple peptide synthesizer. Mass spectrometry of dye-labeled peptides was performed using an AutoFlex II MALDI-TOF (Bruker Daltonics), employing α-cyano-4-hydroxycinnamic acid (CHCA) as matrix. HPLC of the same sample was accomplished using a C18 column with a gradient of 0.1% TFA in water to 0.1% TFA in acetonitrile for 20 minutes at a flow rate of 1.5 mL/min.
Autoflex 2 maldi tof
Manufactured by Bruker
Sourced in Germany
The Autoflex II MALDI-TOF is a mass spectrometry instrument for the analysis of biomolecules. It utilizes Matrix-Assisted Laser Desorption/Ionization (MALDI) technique coupled with Time-of-Flight (TOF) mass analyzer to detect and identify a wide range of analytes, including proteins, peptides, and other biomolecules.
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Lab products found in correlation
3 protocols using autoflex 2 maldi tof
1
Synthesis and Characterization of Labeled Bim BH3 Peptides
2
MALDI-TOF MS Analysis of Protein Separation
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The matrix was prepared by dissolving 2,5-dihydroxybenzoïque (DHB) (2g.L-1) in 0.1% trifluoroacetic acid/acetonitrile (TFA/ACN) (30/70). Fraction collection was realized using Ground Steel MALDI target (Bruker Daltonics, Bremen, Germany). Mass spectra of the CE fractions were recorded using an Autoflex II MALDI-TOF (Bruker Daltonics, Bremen, Germany), operating in reflector mode and with FlexControl software. Positively charged ions were detected and sums of 2000 singleshot spectra were acquired automatically from each sample by using the AutoXecute software. For Topdown approach, sums of 15000 single-shot spectra were acquired automatically from each sample.
Data processing was performed with FlexAnalysis 3.0 provided by the mass spectrometer manufacturer. All spectra were calibrated according an external calibration using Protein calibration standard I (Bruker Daltonics, Bremen, Germany) for intact protein separation.
Data processing was performed with FlexAnalysis 3.0 provided by the mass spectrometer manufacturer. All spectra were calibrated according an external calibration using Protein calibration standard I (Bruker Daltonics, Bremen, Germany) for intact protein separation.
3
MALDI-TOF Analysis of CZE Fractions
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The matrix was prepared by dissolving 2,5-dihydroxybenzoic acid (DHB) (2g/L) in 0.1% trifluoroacetic acid/acetonitrile (TFA/ACN) (30/70)(v/v). Fraction collection was realized using Ground Steel MALDI target (Bruker Daltonics, Bremen, Germany). Mass spectra of the CZE fractions were recorded using an Autoflex II MALDI-TOF (Bruker Daltonics, Bremen, Germany), operating in reflector mode and with FlexControl software. Positively charged ions were detected and sums of 1500 single-shot spectra were acquired automatically from each sample by using the AutoXecute software.
Data processing was performed with FlexAnalysis 3.0 (Bruker Daltonics, Bremen, Germany). All spectra were calibrated by external calibration using Protein calibration standard I (Bruker Daltonics, Bremen, Germany) for intact protein separation.
Data processing was performed with FlexAnalysis 3.0 (Bruker Daltonics, Bremen, Germany). All spectra were calibrated by external calibration using Protein calibration standard I (Bruker Daltonics, Bremen, Germany) for intact protein separation.
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