Matrix-assisted laser desorption/ionization mass spectra (MALDIMS) and electrospray ionization mass spectra (ESIMS) of obtained oligosaccharides were recorded with an Ultra Flex III MALDI-TOF/TOF mass spectrometer (Bruker, Bremen, MA, Germany) and with a Maxis Impact LC Q-TOF mass spectrometer (Bruker, Bremen, MA, Germany), respectively, in the modes described by us earlier [10 (link),26 (link)].
Ultraflex 3 maldi tof tof mass spectrometer
Manufactured by Bruker
Sourced in Germany, United States
The Ultraflex III MALDI-TOF/TOF mass spectrometer is a versatile laboratory instrument designed for high-performance mass spectrometric analysis. It utilizes matrix-assisted laser desorption/ionization (MALDI) and time-of-flight (TOF) technologies to provide accurate mass measurements and tandem mass spectrometry (MS/MS) capabilities for the identification and characterization of a wide range of analytes.
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Lab products found in correlation
Smart beam, by Bruker (3 mentions)
Flexanalysis 3, by Bruker (2 mentions)
Mascot, by Matrix Science (2 mentions)
Flexanalysis software, by Bruker (2 mentions)
Maxis impact lc qtof mass spectrometer, by Bruker (1 mentions)
Imagemaster 2d platinum software, by GE Healthcare (1 mentions)
Scaffold program, by Proteome Software (1 mentions)
Mascot program, by Matrix Science (1 mentions)
Flexanalysis software version 3, by Bruker (1 mentions)
Peptide calibration mix 2, by Bruker (1 mentions)
Bca protein assay kit, by Thermo Fisher Scientific (1 mentions)
Polished steel target plate, by Bruker (1 mentions)
Flexcontrol software, by Bruker (1 mentions)
Peptide calibration standard, by Bruker (1 mentions)
Coomassie blue g 250, by Merck Group (1 mentions)
C18 ziptip, by Merck Group (1 mentions)
Peptide standard, by Bruker (1 mentions)
Silica gel 60, by Merck Group (1 mentions)
Orbitrap elite mass spectrometer, by Thermo Fisher Scientific (1 mentions)
Ziptip c4 tips, by Merck Group (1 mentions)
29 protocols using ultraflex 3 maldi tof tof mass spectrometer
1
Mass Spectrometric Analysis of Oligosaccharides
2
MALDI Analysis of HttQ44-SUMO Protein
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Unmodified (∼49 μM) and N-terminally acetylated recombinant, uncleaved HttQ44-SUMO (∼33 μM) in sizing buffer were diluted 1:10 using Milli-Q water. The diluted sample was then mixed with matrix consisting of saturated sinapic acid solution in a mixture of 30% acetonitrile and 70% Milli-Q-grade water containing 0.1% trifluoroacetic acid. MALDI mass spectra were collected using a Bruker Ultraflex III MALDI-TOF-TOF mass spectrometer with a molecular weight window of 5 to 21 kDa.
3
Peptide Mass Fingerprinting for Protein ID
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Protein identification was carried out by peptide mass fingerprinting55 (link)56 on an Ultraflex III MALDI-TOF/TOF mass spectrometer (Bruker Daltonics, Billerica, MA) as detailed in Supplementary Methods .
4
MALDI-TOF MS Peptide Analysis Protocol
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MALDI-TOF MS spectra of peptides were recorded using an Ultraflex III MALDI-TOF/TOF mass spectrometer (Bruker, Bremen, Germany) with a nitrogen laser (Smart Beam, 355 nm), reflector and potential LIFT tandem modes of operation. Sinapinic acid was used as a matrix. External calibration was employed using a peptide InhVJ with m/z 6107 [43 (link)] and its doubly-charged variant at m/z 3053.
5
MALDI-TOF/TOF Mass Spectrometry Analysis
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Bruker Ultraflex III MALDI-TOF/TOF mass Spectrometer (Bruker Daltonics, Leipzig, Germany) operating in reflectron mode with a 20 kV accelerating voltage and 23 kV reflecting voltage. A saturated solution of α-cyano-4-hydroxycinnamic acid in 50% acetonitrile and 0.1% trifluoroacetic acid was used as the matrix. The matrix solution (1µl) and sample solution at a ratio of 1:1 was applied onto the Score384 target well. A standard peptide calibration mix in the mass range 800-3,200 Da (Bruker Daltonics) was analyzed for external calibration of the mass spectrometer. The calibration mix contained: Angiotensin II, angiotensin I, substance P, bombesin, ACTH clip 1-17, ACTH clip 18-39 and somatostatin 28. A series of eight samples were spotted around one external calibration mixture. The SNAP algorithm (S/N threshold: 5; Quality Factor Threshold: 30) in Flex Analysis 3.0 (Bruker Daltonics) was used to identify the 100 most prominent peaks in the mass range m/z 700-4,000. The subsequent MS/MS analysis was performed in a data-dependent manner and the five most abundant ions fulfilling certain preset criteria (S/N higher than 3 and Quality Factor higher than 30) were subjected to high energy collision-induced dissociation analysis. The collision energy was set to 1 keV and nitrogen was used as the collision gas.
6
MALDI-TOF Mass Spectrometry of Digestion Products
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Digestion products from the SGF assays were analyzed by Matrix-assisted laser desorption/ionization time of flight (MALDI TOF) mass spectrometry. Samples were pre-incubated with 0.5 μl of 40 mM DTT for 20 min on the ground steel plate to reduce disulfide bonds. The samples were subsequently mixed with 2,5-dihydroxybenzoic acid (DHB) and the mass to charge ratio was measured for each sample using a Bruker Daltonics Ultraflex III MALDI-TOF/TOF Mass Spectrometer.
7
MALDI-TOF MS Peptide Analysis Protocol
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MALDI-TOF MS spectra of peptides were recorded using an Ultra Flex III MALDI-TOF/TOF mass spectrometer (Bruker, Bremen, Germany) with a nitrogen laser SmartBeam (355 nm), reflector, and potential LIFT tandem modes of operation. Sinapinic acid was used as the matrix. External calibration was employed using a peptide InhVJ with m/z 6107 [72 (link)] and its double-charged variant at m/z 3053.
8
Bovidae Protein Identification via MALDI-TOF
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Peptide masses of the samples were obtained using an Ultraflex III MALDI TOF/TOF mass spectrometer (Bruker Daltonics, Bremen, Germany) and then screened against the Bovidae database deposited in UniProt using the MASCOT program (Matrix Science, London, UK) and a MASCOT Peptide Mass Fingerprinting database search. An accuracy of 0.5 Da was used in the search criteria. Trypsin was set as an enzyme with one allowed miscleavage. The fixed modification and variable modification factors used were carbamidomethyl and oxidation, respectively. The numbers of peptide matches, sequence coverage, molecular weight (MW), and isoelectric point (pI) were used to evaluate the database search results. The Scaffold program (Proteome Software, Portland, OR) was used to validate the proteins identified by the MASCOT program, with the identity for both proteins and peptides equal to 100%.
Protein abundance was quantified by spot densitometry analysis using ImageMaster 2D Platinum Software (GE Health Care, Little Chalfont-UK). The software used powerful algorithms for efficient spot detection, accurate spot quantification, and an accurate statistical comparison of spot density across gels.
Protein abundance was quantified by spot densitometry analysis using ImageMaster 2D Platinum Software (GE Health Care, Little Chalfont-UK). The software used powerful algorithms for efficient spot detection, accurate spot quantification, and an accurate statistical comparison of spot density across gels.
9
MALDI-TOF MS Analysis of Peptide Fractions
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MALDI-TOF MS spectra of peptide fractions after RP-HPLC were recorded using an Ultra Flex III MALDI-TOF/TOF mass spectrometer (Bruker, Bremen, Germany) with a nitrogen laser (Smart Beam, 355 nm), reflector and potential LIFT tandem modes of operation. Sinapinic acid was used as a matrix.
10
MALDI-TOF Mass Spectrometry of Oligonucleotides
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Acetaldehyde (10 µL) was reacted at room temperature for 1 h with 10 µM 15-mer oligo with GG, which had been prepared in 100 µL of water. An aliquot (2 µL) of the reaction mixture was spotted on a predried 3-hydroxypicolinic acid matrix, dried a second time in ambient conditions, and analyzed on a Bruker Ultraflex III MALDI TOF/TOF mass spectrometer. MALDI TOF mass spectra of purified unreacted oligonucleotides were also collected with the same instrument and matrix.
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