Spots of interest were excised and digested in-gel with trypsin for further protein identification according to previously described procedures [51 (link)]. After digestion, the tryptic peptides were acidified with 0.5% TFA and loaded onto an MTP AnchorChipTM 600/384 TF (Bruker-Daltonik, Bremen, Germany). MS analysis was performed on an UltraflexTM MALDI-TOF mass spectrometer (Bruker-Daltonik). Monoisotopic peptide masses were assigned and used for database searches with the MASCOT search engine (Matrix Science, London, UK). Search parameters were set as follows: a maximum allowed peptide mass error of 50 ppm, and consideration of one incomplete cleavage per peptide.
Mtp anchorchip 600 384 tf
Manufactured by Bruker
Sourced in Germany
The MTP AnchorChip™ 600/384 TF is a specialized sample preparation plate designed for use with Bruker's MALDI-TOF mass spectrometry systems. It features a 600-well format with a 384-well target area, enabling high-throughput sample analysis. The product's core function is to provide a standardized and consistent platform for sample preparation and presentation in MALDI-TOF experiments.
Automatically generated - may contain errors
Lab products found in correlation
Ultraflex maldi tof mass spectrometer, by Bruker (7 mentions)
Mascot search engine, by Matrix Science (4 mentions)
Iodoacetamide, by Cytiva (1 mentions)
Potassium ferricyanide, by Merck Group (1 mentions)
Sodium thiosulfate, by Merck Group (1 mentions)
Trypsin, by Promega (1 mentions)
Biotools 3, by Bruker (1 mentions)
Ultraflex maldi tof ms, by Bruker (1 mentions)
Flexcontrol software, by Bruker (1 mentions)
8 protocols using mtp anchorchip 600 384 tf
1
Proteomic Analysis via MALDI-TOF MS
2
In-Gel Tryptic Digestion and MALDI-TOF MS
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Spots of interest were excised and in-gel digested with trypsin for further protein identification according to previously described procedures [32 (link)]. After digestion, the tryptic peptides were acidified with 0.5% TFA and loaded onto an MTP AnchorChipTM 600/384 TF (Bruker-Daltonik, Bremen, Germany). MS analysis was performed on an UltraflexTM MALDI-TOF mass spectrometer (Bruker-Daltonik). Monoisotopic peptide masses were assigned and used for database searches with the MASCOT search engine (Matrix Science, London, UK). Search parameters were set as follows: a maximum allowed peptide mass error of 50 ppm, and consideration of one incomplete cleavage per peptide.
3
Proteomic Identification of Differentially Expressed Proteins
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More than 1.5-fold increased or decreased silver-stained spots were excised and in-gel digested with trypsin according to procedures described previously [17 (link)-19 (link)]. Briefly, the gels were destained by 1% potassium ferricyanide and 1.6% sodium thiosulfate (Sigma, St. Louis, MO, USA). The proteins were then reduced with 25 mM NH4HCO3 containing 10 mM DTT (Biosynth, Switzerland) at 60°C for 30 min and alkylated with 55 mM iodoacetamide (Amersham Biosciences, Amersham, Buckinghamshire, UK) at room temperature for 30 min. After reduction and alkylation, the proteins were digested with trypsin (Promega, Madison, WI, USA) (20 mg/ml) at 37°C overnight. After digestion, the tryptic peptides were acidified with 0.5% TCA and loaded onto an MTP Anchor Chip™ 600/384 TF (Bruker Daltonik GmbH, Bremen, Germany). MALDI-TOF MS analysis was performed on an Ultraflex™ MALDI-TOF mass spectrometer (Bruker Daltonik). Mono-isotopic peptide masses were assigned and used for database searches with the MASCOT search engine (http://www.matrixscience.com ) (Matrix Science, London, UK).
4
Protein Identification by MALDI-TOF MS
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Targeted protein spots were excised from the gels and digested with trypsin as previously described [27 (link)]. The tryptic peptides were acidified with 0.5% trifluoroacetic acid (TFA) and loaded onto an MTP AnchorChip™ 600/384 TF (Bruker-Daltonik, Bremen, Germany) after digestion. MS analysis was conducted using the Ultraflex™ MALDI-TOF mass spectrometer (Bruker-Daltonik). Monoisotopic peptide masses were assigned and utilized for database searches with the MASCOT search engine (version 2.2.04, Matrix Science, London, UK). Search parameters were enacted as follows: a maximum allowed peptide mass error of 50 ppm, and consideration of one incomplete cleavage per peptide.
5
Proteomic Profiling by MALDI-TOF Mass Spectrometry
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Silver-stained spots were excised and in-gel-digested with trypsin according to previously described procedures [32 (link)]. Briefly, spots showing differential expression were manually excised and digested with trypsin (20 μg/mL) at 37°C overnight. After digestion, tryptic peptides were acidified with 0.5% TFA and loaded onto an MTP AnchorChip™ 600/384 TF (Bruker-Daltonik, Bremen, Germany). The MS analysis was performed on an Ultraflex™ MALDI-TOF mass spectrometer (Bruker-Daltonik). Monoisotopic peptide masses were assigned and used for Swiss-Prot primary sequence database searches with the BioTools 3.2 software (Bruker-Daltonik) and the Mascot search engine (http://www.matrixscience.com ) (Matrix Science, London, UK). Search parameters were set as follows: a maximum allowed peptide mass error of 50 ppm and consideration of 1 incomplete cleavage per peptide. For MS/MS, the 3 most intense precursor ions with a signal/noise ratio of > 25 were selected after exclusion of the common background signal. The MS/MS mode was operated at 1 keV, and products of metastable decomposition at elevated laser power were detected. PMF data were acquired with close internal calibration and MS/MS data using the default instrument calibration.
6
Mass spectrometric analysis of AKT-CLLV-1 adducts
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Synthetic AKT peptides were dissolved in PBS. The mixtures of AKT peptides (120 μM) and CLLV-1 (60 μM) were incubated at 25 °C for 2 h. The AKT peptides and their CLLV-1 adducts were detected using matrix-assisted laser desorption/ionization time of flight mass spectrometer (MALDI-TOF MS). The AKT peptides and their CLLV-1 adducts were mixed with α-Cyano-4-hydroxycinnamic acid (CHCA) matrix (2 mg/mL in 80% acetonitrile containing 0.1% trichloroacetic acid) and loaded onto an MTP AnchorChip™ 600/384 TF (Bruker Daltonics GmbH, Bremen, Germany). After the crystallization of the peptides and the matrix, the samples were analyzed by an Ultraflex™ MALDI-TOF MS (Bruker Daltonics GmbH), controlled by the FlexControl software (v.2.2; Bruker Daltonics GmbH). Data processing was performed and monoisotopic peptide mass was acquired using the FlexAnalysis 2.4 peak-picking software (Bruker Daltonics GmbH).
7
In-Gel Tryptic Digestion and MALDI-TOF MS
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Protein spots of interest were excised and in-gel digested with trypsin as previously described [39 (link)]. Briefly, tryptic peptides were acidified with 0.5% TFA and loaded onto an MTP AnchorChip™ 600/384 TF (Bruker-Daltonik, Bremen, Germany). The MS analysis was performed on an Ultraflex™ MALDI-TOF mass spectrometer (Bruker-Daltonik, Bremen, Germany) and the monoisotopic peptide masses were applied for database searches with the MASCOT search engine [http://www.matrixscience.com ].
8
MALDI-TOF Mass Spectrometry of Tryptic Peptides
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Spots of interest were excised and in-gel digested with trypsin according to previously described procedures [49 (link), 51 (link)]. After digestion, the tryptic peptides were acidified with 0.5% TCA and loaded onto an MTP AnchorChip™ 600/384 TF (Bruker-Daltonik, Bremen, Germany). MS analysis was performed on an Ultraflex™ MALDI-TOF mass spectrometer (Bruker-Daltonik). Spectra were collected and calibrated by four point internal calibration (m/z 956.5355, 1296.6860, 1758.9335, 2465.198). Monoisotopic peptide masses were assigned and used for database searches with the MASCOT search engine (http://www.matrixscience.com ) (Matrix Science, London). Search parameters were set as follows: a maximum allowed peptide mass error of 50 ppm, and consideration of one incomplete cleavage per peptide. For TOF/TOF, the three most intense precursor ions with a signal/noise ratio of >25 were selected after exclusion of common background signals [53 (link)].
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