Aplikacje MS

Broszury dotyczące rozwiązań dedykowanych wybranym obszarom analityczym:

Poniżej znajdziecie Państwo spis dostępnych w formie elektronicznej not aplikacyjnych i technicznych opublikowanych przez firmę Bruker w zakresie spektrometrii mas. Zostały one podzielone na sekcje wg typu instrumentów, z pomocą których uzyskano dane do publikacji. Są to kolejno:

  • LC-MS dotyczące pułapek jonowych esquire/HCT/amaZon, potrójnego kwadrupola EVOQ oraz naszych Q-TOFów
  • ESI-(Q-)TOF dotyczące instrumentów serii micrOTOF(-Q), impact i maXis
  • MALDI-TOF(/TOF) dotyczące serii instrumentów flex
  • Qh-FTMS dotyczące spektrometrów apex i solariX
  • noty techniczne traktujące o technologiach i funkcjach wykorzystanych w spektrometrach firmy Bruker

Można je pobrać klikając na numer noty znajdujący się po jej tytule. Jeśli któraś z publikacji wzbudzi Państwa zainteresowanie, uprzejmie prosimy o kontakt. Postaramy się odpowiedzieć na wszystkie zapytania.

LC-MS

  • Investigating Non-Covalent Interactions of Proteins by Ion Trap ESI/MS – LCMS02
  • LC/MS Analysis of Aflatoxins in Food Samples Using an Ion Trap – LCMS09
  • Investigation of Carotinoids in Spinach Using LC/APCI-MS – LCMS10
  • Quantification of Morphine, 6-Monoacetyl-morphine, Codeine and Nalorphine using an Ion Trap LC-MS – LCMS11
  • On-line, Near-orthogonal Nano-Electrospray coupled with Ion Trap MS for Proteomic Analysis – LCMS12
  • Quantitation of Anesthetic Agents in Rat Plasma by ESI-Ion Trap MS – LCMS15
  • Application of LC/ESI-Ion Trap MS for Quantitation of Ochratoxin in Plant Extracts – LCMS16
  • Identification and Quantitation of Microcystins in Water Samples or Extracts from Cyanobacterias – LCMS17
  • Structural Characterization of Oligosaccharide Derivatives using LC/ESI Ion Trap MS – LCMS18
  • Usage of LC/APCI-MS/MS for Quantitation of Patulin in Food Samples – LCMS19
  • Application of LC/Electrospray Ion Trap Mass Spectrometry for Identification and Quantification of Pesticides in Complex Matrices – LCMS20
  • Online Coupling of GPC and ESI-MS for Characterization of Synthetic Polymers using an Ion Trap – LCMS21
  • CE/MS/MS of Enzymatic Digests and Peptides with an Ion Trap – LCMS22
  • The Use of Non-volatile Buffers in LC-MS/MS – LCMS23
  • Automated Molecular Weight Determination from Adduct Ions in ESI Spectra for Library Search – LCMS24
  • Protein Identification in the Sub-femtomol Range using NanoESI-Ion Trap MS – LCMS25
  • Custom Mass Spectral Library for Rapid Identification of Phenolic Compounds Analyzed by the esquire3000plus – LCMS26
  • Confirming the Primary Sequence of Recombinant Proteins by Electrospray Mass Spectrometry – LCMS31
  • Mass spectrometric analysis of head-to-tail connected cyclic peptides – LCMS32
  • De Novo Sequencing using Peak Parking in Combination with NanoLC-Ion Trap Mass Spectrometry – LCMS33
  • Comprehensive 2D NanoLC as front-end technique for MS in Proteomics – LCMS34
  • Application of LC/APCI Ion Trap Tandem MS for the Multiresidue Analysis of Pesticides in Water – LCMS35
  • Identification of BADGE and BFDGE in Extracts of Food or Epoxy Resin Food Can Coatings using LC/APCI Ion Trap Tandem MS – LCMS36
  • De Novo Sequencing of Tryptic Peptides using MALDI-TOF/TOF MS and nanoESI-Ion Trap MS – LCMS37/MT66
  • High sensitivity protein identification using an AP MALDI source on the esquire – LCMS38
  • Novel Strategies for Metabolite Identification using HPLC-Ion Trap Mass Spectrometry and the MetaboliteTools software – LCMS39
  • PROTEINEER-LC: Interfacing LC to ESI- and MALDI-MS/MS Analysis Towards High-Throughput and High Content Proteomics – LCMS40/MT69
  • A new De-novo Sequencing Tool for sophisticated MS/MS Data Analysis beyond Protein Identification – LCMS41
  • Rapid Identification of Testosterone Metabolites using Accurate Mass and MS/MS Data – LCMS42/ET07
  • Identification of Proteins from Taxus baccata: A Species with a Non-Sequenced Genome – LCMS43
  • Protein assignment to predicted ORFs of an environmental Bacterium with sequenced Genome: Challenges and Solutions – LCMS44/MT73
  • Application of MetaboliteTools™ for the Comparison of Capsaicinoid Profiles in Different Chili Peppers – LCMS45
  • Automatically identifying posttranslational modifications and transpeptidation products from MS/MS spectra using the PTM-Explorer software – LCMS46/MT81
  • New Approach for Characterization of Post Translational Modified Peptides Using Ion Trap MS with Combined ETD/CID Fragmentation – LCMS47/LCGC0905
  • Structure Elucidation of Steroidal Saponins Using MS(n) Analysis – LCMS48
  • Melamine and Cyanuric Acid Detection in 5 Minutes using LCMS – LCMS49
  • Identification of Multiple Proteins Present in a Standard Mixture: Study of the ABRF Proteomics Standards Research Group 2006 – LCMS50/MT84
  • “Zero Delay” Polarity Switching for Ultra-fast MS/MS Screening Applications – LCMS51
  • Top-Down Proteomics with ETD/PTR: Essential Data Quality Improvement by Increased Resolution and Scan Speed of the amaZon Ion Trap – LCMS52
  • Ion Funnel Transmission Increases the Number of Protein Identifications in Complex Proteomics Samples – LCMS53
  • „Replay” Significantly Increases the Number of Protein Assignments from Complex Proteomics Samples – LCMS54
  • Natural Organic Dye MSn Library For Museum and Art Conservation Application – LCMS55
  • ICPL Labeling in Functional Proteomics Experiments: Substrate Identification of the Extracellular Protease ADAMTS1 using SDS-PAGE LC-MS/MS – LCMS56
  • In-depth Characterization of Neutral and Acidic Glycopeptides by ZIC-HILIC Enrichment and Mass Spectrometry – LCMS57/MT107
  • Biomarker Discovery and Identification by MALDI Molecular Tissue Imaging and Top-down Sequencing – LCMS59/MT108
  • Quantitative Analysis of Perchlorate using the Bruker amaZon SL Ion Trap Mass Spectrometer – LCMS60
  • Identification and Quantitation of four Aflatoxins using the Bruker amaZon SL Ion Trap MS – LCMS61
  • Walk-Up Ion Trap Mass Spectrometer System in a Multi-User Environment Using Compass OpenAccess Software – LCMS62
  • Improving Low Abundance Protein Identification in Complex Proteome Samples – LCMS63
  • amaZon speed – accelerating access to proteomic information – LCMS64
  • 2500 Protein Identified from a Human cell Lysate with Complementary MALDI and ESI Data – LCMS65
  • Straightforward N-glycopeptide analysis combining fast ion trap data acquisition with new ProteinScape functionalities – LCMS66
  • 3.500 Proteins Identified from a Human Cell Lysate Using Camplementary MALDI and ESI Data – LCMS67
  • amaZon speed – Improved Speed and Efficiency in Small Molecule LC-MS(n) Experiments Using a New Automated Panorama Fragmentation Mode – LCMS68
  • Detailed Structural Characterization of IgG N-glycans Using Porous Graphitic Carbon LC-ESI Ion Trap MS/MS – LCMS70
  • Identification of 2.500 Proteins from a HeLa Cell Culture Sample Using the amaZon speed ETD system – LCMS71
  • Identification and Characterization of PTMs from A Complex Peptide Mixture Using the amaZon speed ETD Ion Trap System – LCMS75
  • Label-free Quantification of Phosphorylation Occupancy in a Phosphoprotein with Multiple Phosphorylation Sites – LCMS77
  • Automated Analysis of Protein Sequence Variants by LC-MS Under the Control of BioPharma Compass – LCMS78
  • Metabolic Profiling of Different Coffee Types on the Bruker compact QTOF System – LCMS79
  • Simultaneous Quantitative and Qualitative Measurements in a Single Workflow to Increase Productivity in Primary Drug Metabolism Investigations – LCMS80
  • High Throughput Quantitative and Qualitative DMPK Measurements – LCMS82
  • Smart MRM with Electron Transfer Dissociation of Hemoglobin in Clinical Samples – LCMS83
  • Combining PGC-LC ESI and MS2/MS3 ion trap analysis for structural characterization of sulphated O-glycans – LCMS84
  • Plant Metabolomics Research Highlight: Prof. Lloyd W. Sumner combines UHPLC-MS-SPE-NMR and Prof. Kazuki Saito employs FT-ICR-MS in novel strategies to identify unknown plant metabolites – LCMS85
  • Food Authenticity – Classification of Coffee Types Based on LC-MS – LCMS86
  • Automated Acquisition and Analysis of Data for Monitoring Protein Conjugation by LC-MS Using BioPharma Compass – LCMS87
  • Isotopic Ratio Outlier Analysis (IROA®) coupled with the Bruker maXis 4G QTOF to investigate changes in the secondary metabolite profiles of Myxobacteria – LCMS88
  • High quantification efficiency in plasma targeted proteomics with a full-capability discovery Q-TOF platform – LCMS89
  • amaZon ion trap: An all-rounder for in-depth structure elucidation of carbohydrates – LCMS90
  • Toxtyper – a Comprehensive LC-MSn Screening Solution for Clinical and Forensic Toxicology – LCMS91
  • Interlaboratory Tests Demonstrate the Robustness and Transferability of the Toxtyper Workflow – LCMS92
  • amaZon speed ETD: Exploring glycopeptides in protein mixtures using Fragment Triggered ETD and CaptiveSpray nanoBooster – LCMS93
  • Native and Subunit Analysis of an Antibody Drug Conjugate Model with Ultra-High Resolution Quadrupole Time-of-Flight Mass Spectrometry – LCMS94
  • Quantitative Determination of Serum 25-OH-vitamin D3/D2 using the Tecan AC Extraction Plate™ and the amaZon speed Ion Trap – LCMS95
  • Adopting Forensic Analyses to Specific Lab Needs – Identifying Psychotropics in Serum Using the Toxtyper Open Library Concept – LCMS96
  • Quantitation of 250 Pesticides in Fruit Juices with Positive/Negative Switching LC-MS/MS – LCMS97
  • Comprehensive detection and identification of synthetic cannabinoids using the Toxtyper platform – LCMS99
  • Reduction of matrix effects using LC-MS/MS with online extraction for quantitation of antibiotics in milk – LCMS100
  • Enabling Characterization of Protein Therapeutics Derived from Xpress CF™ Technology with LC-ESI UHR QTOF/MS – LCMS101
  • Analysis of Environmental Samples with a Novel Atmospheric Pressure GC Source Coupled to High-Resolution TOF-MS Analysis – LCMS102
  • Online Analysis of 25-OH-Vitamin D2/D3 in Plasma and Serum with the EVOQ LC-Triple Quad – LCMS103
  • Monitoring multi-class pollutants in surface and groundwater with LC-MS/MS – LCMS104
  • Online Analysis of Immunosuppressants in Whole Blood with the EVOQ Tandem Quadrupole Mass Spectrometer – LCMS105
  • Efficacy of Enhanced Confirmation Criteria to Reduce False Positive Detections in Forensic Screening Using LC-QTOF Mass Spectrometry – LCMS106
  • Quantitation of Benzodiazepine and Z-drug Hypnotics Using High Resolution, Liquid Chromatography-Quadrupole Time of Flight Mass Spectrometry – LCMS107
  • Quantitation of benzodiazepines and Z-drugs in serum with the EVOQ LC triple quadrupole mass spectrometer – LCMS108
  • A Simple and Accurate Method for the Rapid Quantitation of Drugs of Abuse in Urine Using Liquid Chromatography Time of Flight (LC-TOF) Mass Spectrometry – LCMS109
  • Development of a Targeted Quantitative LC-MS/MS Method for 431 Positive and Negative Ion Pesticides in a Single Analysis – LCMS110
  • Enhanced Accurate Mass Subunit Analysis with High Sequence Coverage LC-CID-MS/MS and LC-ETD-MS/MS on maXis II ETD – LCMS111
  • A Fully Automated Two-Step Procedure for Quality Control of Synthetic Peptides – LCMS112

 

ESI-(Q-)TOF

  • CE-ESI-TOF/MS: Combining separaton efficiency with the mass accuracy of the micrOTOF – ET05
  • Rapid Identification of Testosterone Metabolites using Accurate Mass and MS/MS Data – ET07/LCMS42
  • Study of noncovalent protein/ligand complexes using micrOTOF mass spectrometer – ET08
  • Principal Component Analysis of Urine Samples Based on ESI–TOF–MS Data – ET09/LCGC0306
  • Quantification of Proteomics Samples using ESI-Qq-TOF Mass Spectrometry – ET11
  • Multi Target compound analysis of multiple pesticides – ET12
  • De Novo Formula Generation with „sub-ppm” confidence using Compass OpenAccess and the micrOTOF – ET13
  • Targeted Protein Quantification: Determination of Target-Proteins in a Complex Mixture – ET14
  • Analysis of Complex Pharmaceutical Mixtures by maXis with Fast Chromatography – ET15
  • Improved Peptide Identification with an Ultra High Resolution Quadrupole Time of Flight MS – ET16
  • Characterization of the N-glycosylation pattern of Antibodies by ESI and MALDI mass spectrometry – ET17/MT99
  • Rapid Quality Control of Biopharmaceutical Products – ET18
  • Metabolic profiling of tea extracts by high-resolution LC in combination with maXis UHR-TOF MS analysis – ET19
  • BioPharma Compass: A fully Automated Solution for Characterization and QC of Intact and Digested Proteins – ET20
  • Challenges in Metabolomics addressed by targeted and untargeted UHR-Q-TOF analysis – ET21
  • Metabolic Profiling of a Corynebacterium glutamicum prpD2 by GC-APCI High Resolution Q-TOF Analysis – ET22
  • Accurate Molecular Formula Determination and Identification Of Molecules With >1100 m/z with UHR-TOF – ET23
  • ESI-Q-TOF MS/MS study of poly(2-oxazoline)s – ET25
  • Novel approaches for small molecule identification in Metabolomics research – ET26
  • Sensitive Detection of Chloramphenicol in Food Using the New ionBooster Source with maXis impact – ET27
  • Enhanced Determination of Alcohol Biomarkers Using Mass Spectrometry with the New ionBooster Source – ET28
  • Screening for novel natural products from myxobacteria using LC-MS and LC-NMR – ET29
  • Metabolic profiling of Arabidopsis thaliana secondary metabolites using a maXis impact – ET30
  • Drug Metabolite Detection and Identification Combining Bruker MetaboliteTools with Lhasa Limited’s Meteor Software – ET31
  • Automated Antibody Verification for Lead Discovery – ET32
  • Metabolomics Studies on Yeast Arginine Synthesis Pathway Mutants Using maXis impact with ionBooster – ET33
  • micrOTOF-Q II for Obtaining the Relative Ligand Binding Strengths in IrIII Complexes – ET34
  • ESI and MALDI Tandem Mass Spectrometry of Poly(ethylene imine)s: A Comparison Study for Structural Characterization – ET35
  • Tandem Mass Spectrometry of Poly(methylacrylate)s by ESI, APCI and MALDI – ET37
  • Compass PathwayScreener – Metabolic-pathway–directed targeted metabolomics – ET38
  • DirectProbe Atmospheric Pressure Photo Ionization /Atmospheric Pressure Chemical Ionization High Resolution Mass Spectrometry for Fast Screening of Flame Retardants and Plasticizers in Plastics of Electronic Products – ET39

 

MALDI-TOF(/TOF)

  • Direct MALDI-TOF-MS Analysis of Microorganisms – MT51
  • Detection Limits of MALDI-TOF PSD for Peptide Sequencing from Protein Digests – MT52
  • N-terminal Derivatization of Tryptic Peptides for de novo Sequencing by PSD – MT53
  • ApoE and A2M genotyping by MALDI-TOF mass spectrometry for determination of Alzheimer disease risk – MT54
  • Genotyping of risk factors for cardiovascular disease by MALDI-TOF MS – MT55
  • GOOD assay genotyping of Single Nucleotide Polymorphisms (SNPs) – MT56
  • Reflector In-Source-Decay (ISD) MALDI-TOF MS: A Powerful Tool for N-terminal Sequence Characterization of Proteins – MT57
  • Hydrophilic Anchors: High-Throughput Protein Identification in the Subfemtomol Range – MT58
  • Control of Co-Polymer Synthesis by Means of MALDI-TOF MS – MT59
  • Prestructured MALDI Sample Supports: Sample Washing and Recrystallization – MT60
  • Automated sample preparation for genotyping of DNA polymorphisms via MALDI-TOF mass spectrometry – MT61
  • The GOOD assay – a procedure for SNP genotyping using MALDI-TOF mass spectrometry – MT62
  • Automated genopure DNA purification for MALDI-TOF-MS based genotyping and sequencing of the blood clotting factor V (F5) Leiden allele – MT63
  • Automated In-Gel Digestion and MALDI Sample Preparation using the PROTEINEER dp Station – MT64
  • MALDI-TOF/TOF MS for High Throughput and High Success Rate in Industrial Proteomics – MT65
  • De Novo Sequencing of Tryptic Peptides using MALDI-TOF/TOF MS and nanoESI-Ion Trap MS – MT66/LCMS37
  • Proteomics application exercise of the Swiss Proteomics Society: Structural characterization of a recombinant protein – MT67
  • MALDI-TOF-MS based genotyping and DNA sequencing of the coding SNP A896G in the TLR4 gene: Automated genopure and genostrep DNA purification on the puredisk robotic platform – MT68
  • PROTEINEER-LC: Interfacing LC to ESI- and MALDI-MS/MS Analysis Towards High-Throughput and High Content Proteomics – MT69/LCMS40
  • Comparison of LID and high Energy CID of Peptides in MALDI-TOF/TOF – MT70
  • LC-MALDI – a powerful tool for high confidence protein identification from protein mixtures – MT71
  • Magnetic Bead based Human Plasma Profiling to Discriminate Acute Lymphatic Leukaemia from Non-Diseased Samples – MT72
  • Protein assignment to predicted ORFs of an environmental Bacterium with sequenced Genome: Challenges and Solutions – MT73/LCMS44
  • Improved SNAP Algorithm: Application for Quantitation of 18O-Labeled Peptides – MT75
  • Automatically Identifying Proteins from 2D Gels using the PROTEINEER line – MT76
  • High Success Protein Identification from Complex Samples with LC-MALDI – MT77
  • ICPL: A new quantitative mass spectrometric method for proteomics – MT78
  • Microorganism identification and classification based on MALDI-TOF MS fingerprinting – MT80
  • Automatically identifying posttranslational modifications and transpeptidation products from MS/MS spectra using PTM-Explorer software – MT81/LCMS46
  • Sensitive Detection of Low Abundant Peptides from Complex Samples with LC-MALDI – MT82
  • Accurate Quantification with ICPL: The Quantification Study of the ABRF Proteomics Research Group – MT83
  • Identification of Multiple Proteins Present in a Standard Mixture: Study of the ABRF Proteomics Standards Research Group 2006 – MT84/LCMS50
  • LC-MALDI based Top-Down profiling: a new tool for biomarker discovery and identification – MT85
  • Quantitative Proteome Analysis by Labeling of Arginine and Lysine with SILAC, SDS-PAGE, and nano-LC-MALDI-TOF/TOF Mass Spectrometry – MT86
  • MALDI Tissue Imaging of Drugs with the ultraflex MALDI TOF/TOF – MT87
  • Rapid MS-analysis of in vitro drug permeability and transport assays using NALDI target plates – MT88
  • Advances in Molecular Histology with the MALDI Molecular Imager – MT89
  • MALDI-TDS: A Coherent MALDI Top-Down-Sequencing Approach Applied to the ABRF-Protein Research Group Study 2008 – MT90
  • High Quality MALDI Imaging of Proteins and Peptides in Small Rodent Organ Tissues – MT91
  • In Vitro Mouse Tissue Imaging of an Anti-Tumor Drug, Temozolomide, with MALDI-TOF/TOF – MT92
  • Small Molecule Drug Imaging of Mouse Tissue by MALDI-TOF/TOF Mass Spectrometry and FTMS – MT93/FTMS38
  • Direct Read-out of Thin Layer Chromatography (TLC) using MALDI-TOF – MT94
  • Edmass™: Top-Down Sequence Validation on a Benchtop MALDI-TOF Mass Spectrometer – MT95
  • Calling N- and C-terminal Protein Sequences with High Confidence and Speed: MALDI-TDS applied to the ABRF-ESRG 2009 Research Study – MT96
  • MALDI Imaging of Proteins at 20µm Resolution On the ultrafleXtreme – MT97
  • Spatially Resolved Tryptic Digest on Tissue using the ImagePrep – MT98
  • Characterization of the N-glycosylation pattern of Antibodies by ESI and MALDI mass spectrometry – MT99/ET17
  • Accelerated nanoLC-MALDI-TOF/TOF Analysis of Complex Proteomics Samples Performed at a New Level of Resolution and Mass Accuracy – MT100
  • High Resolution Lipid Profiling and Identification by Hyphenated HPTLC-MALDI-TOF/TOF – MT101
  • Verification of Terminal Sequences by Edmass Top-Down Sequencing (Edmass TDS) of Intact Proteins using the autoflex speed – MT102
  • FAST-SRM: A new Single Reaction Monitoring Method for Fast, Targeted Drug Distribution Testing in Tissue Sections – MT103
  • MALDI-CID Study of Poly(Methyl Methacrylate) – MT105
  • Isotope-Coded Protein Labeling (ICPL) for Quantitative Proteomics Workflows Compatible with Protein Separation Strategies – MT106
  • In-depth Characterization of Neutral and Acidic Glycopeptides by ZIC-HILIC Enrichment and Mass Spectrometry – MT107/LCMS57
  • Biomarker Discovery and Identification by MALDI Molecular Tissue Imaging and Top-down Sequencing – MT108/LCMS59
  • Concise Interpretation of MALDI Imaging Data by Probablilistic Latent Semantic Analysis (pLSA) – MT111
  • Precise MW Determination of Intact Proteins by Multiple Charge State Analysis of MALDI Generated Ions – MT112
  • MALDI Imaging with Single Cell Resolution at 10 um Pixel Size – MT113/FTMS47
  • Comprehensive Study of O-linked Glycopeptides of Erythropoeitin – MT114
  • MALDI Imaging Success Stories in Clinical Research – Mini Review – MT115/FTMS53
  • High-throughput Screening of Deubiquitylase enzyme (DUB) activity/specificity and inhibitor screening by MALDI-TOF mass spectrometry – MT116

 

Qh-FTMS

  • Accurate Mass Analysis of a Multi-Component Drug Mixture Using Fast Gradient HPLC/ESI/FTMS – FTMS26
  • High Mass Accuracy Approach to Proteomics Using Fourier Transform Mass Spectrometry – FTMS27
  • De Novo Sequencing and Detection of Labile Post-Translational Modifications with Electron Capture Dissociation (ECD) FTMS/MS – FTMS28
  • The Utility of Combining Infrared Multiphoton Dissociation with Fourier Transform Mass Spectrometry – FTMS29
  • The Effect of Combined High Mass Measurement Accuracy and MS/MS in Proteomics with MALDI- and Nano-ESI-FT-ICR Mass Spectrometry – FTMS30
  • Fast Isocratic NanoLC-FT-ICR MS for Protein Identification from Mixtures of Enzymatic Digests – FTMS31
  • High Mass Accuracy MALDI FT-ICR MS for Protein Identification from Mixtures of Enzymatic Digests – FTMS32
  • New APEX-Q Hybrid Qq-FTMS – FTMS33
  • A Top-Down Approach to Characterizing Residue Specific Lysine Reactivity using the APEX-Q FTMS – FTMS34
  • apex-Qe: A Powerful Platform for Molecular Formula Determination – FTMS35
  • Fast Elemental Composition Identifications of Mixtures with Ultra-High-Resolution apex Qe FTMS – FTMS36
  • High Resolution Molecular Imaging of Pharmaceuticals at Therapeutic Levels – FTMS37
  • Small Molecule Drug Imaging of Mouse Tissue by MALDI-TOF/TOF Mass Spectrometry and FTMS – FTMS38/MT93
  • MALDI In-Source Decay for Top-Down Analysis of Proteins using Fourier Transform Mass Spectrometry – FMTS39
  • Expanded Collisional Energy Files for Automated Top Down and Bottom up Analysis on solariX – FMTS40
  • Analysis of Gas Oil by GC/APCI FTMS – FMTS41
  • Analysis of sulfur-rich crude oil and bitumen by FTMS – FMTS44
  • MALDI Imaging with Single Cell Resolution at 10 um Pixel Size – FTMS47/MT113
  • Microbial Imaging Mass Spectrometry With Fourier Transform Ionization Mass Spectrometry – FTMS48
  • Top Down Analysis of Histone H4 – FTMS49
  • Ultrafast Statistical Profiling of Bacterial Metabolite Extracts – FTMS51
  • MALDI Imaging Success Stories in Clinical Research – Mini Review – FTMS53/MT115
  • Laser/Desorption Ionization FT-ICR Mass Spectrometry as a Tool for Statistical Analysis of Crude Oils – FTMS55
  • Reproducibility of Crude Oil Characterization by Flow Injection APPI-FT-ICR Mass Spectrometry – FTMS56

 

noty techniczne

  • PROTEINEER – From 2D gel to Protein Identification and Characterization – TN02
  • ProteinScape: An integrated Bioinformatics Platform for Proteome Analysis – TN03
  • Analysis of Intact Proteins on the microTOF ESI-TOF System – TN04
  • Processing Fluorescent Gels with the PROTEINEER spll – TN05
  • Comparison of LIFT I and LIFT II – TN06
  • Ruggedness of LC-MS/MS Ion Trap Systems Against Matrix Contaminants – TN07
  • Quantitative Analysis by LC-MS/MS Using the HCT Ion Trap Mass Spectrometer – TN09
  • Spot detection from 2D gels utilizing spControl 3.0 – TN10
  • Disposable Prespotted AnchorChip MALDI targets for gel-based and LC-MALDI based proteomics – TN11
  • Innovative smartbeam laser technology enhances MALDI-TOF based proteomics applications – TN12
  • Sample preparation for MALDI-TOF MS using CLINPROT magnetic beads – TN13
  • Precise Mass Performance of the micrOTOF with either Dual-Sprayer Internal Calibration or Highly Stable External Calibration – TN14
  • Effect of different laser beam angles on performance of MALDI TOF with gridless ion optics – TN15
  • Proteome Analysis of a limited Number of Human Cells – TN16
  • A New Device for Automated MALDI Imaging High Performance Sample Preparation – TN18
  • A new automated biosensor system for rapid, nucleic acid-based detection and characterization of microorganisms – TN19
  • Omni Spray (DESI) on Bruker Daltonics API Mass Spectrometers for Neat Sample Analysis – TN21
  • Analyzing small molecule drug compounds by NALDI mass spectrometry – TN22
  • Certainty in Small Molecule Identification by Applying SmartFormula 3D on a UHR-TOF Mass Spectrometer – TN23
  • Extending the Capacity in Modern Spherical High Capacity Ion Traps (HCT) – TN24
  • Simple and Fast Two-Dimensional LC-MS on the Bruker EASY-nLC: EASY-2D – TN25
  • SmartFormula3D – New Dimension in Substance Identification – From Mass Spectrum to Chemical Formula – TN26
  • ProteomeQuant – A Highly Efficient Solution for Biomarker Discovery and Label-free Identification of Regulated Proteins in Biological Systems – TN27
  • maXis High Resolution LC/MS Makes the Most of Ultrafast LC Separations – TN28
  • Redefining MALDI-TOF/TOF Performance – TN31
  • Top-Down Analysis Using the solariX-TD – TN33
  • Rapid Analysis of Complex Mixtures Using the solariX-CM FTMS Platform – TN34
  • amaZon Ion Trap: New Performance Levels Meeting Demanding Analytical Requirements – TN35
  • Automated Acquisition of MALDI-ISD Spectra for the N- and C-terminal Sequence Determination of Intact Proteins – TN36
  • Towards 100% Sequence Coverage in Protein QC: In-depth Characterization of Monoclonal Antibodies Using the Proteinscape Database Software – TN37
  • Fast and Reliable Reaction Yield and Compound Purity Assessment in Synthesis Quality Control – TN38
  • Direct Probe: Instant answers from solid samples – Redefining the routine analysis of crude synthesis samples – TN39
  • Top-Down Characterization of Intact Proteins by Ultra-high Resolution maxis ETD – TN40
  • MTP AnchorChip 1536 TF: A new high capacity MALDI target for improved analysis of complex proteomics samples – TN41
  • Phosphoproteome mapping with the amaZon speed ETD – TN42
  • Targeted Proteomics Using HR-XIC Filtering with Skyline – TN43
  • Increasing Peptide Identification Rates for Proteomics Samples by Controlling Peptide Charge States Using CaptiveSpray nanoBooster – TN44