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Bruker Announces Multiple Placements of MALDI Biotyper Systems with Various German Federal, State and Local Governmental Authorities BREMEN, Germany--(BUSINESS WIRE)-- Bruker today announces ...
MALDI TOF/TOF mass spectrometers are used to reveal amino acid sequence of peptides using post-source decay or high energy collision-induced dissociation (further use see mass spectrometry). MALDI-TOF have been used to characterise post-translational modifications. For example, it has been widely applied to study protein methylation and ...
Bruker Expands Capabilities of MALDI Biotyper Platform for Microbiology Bruker Launches Library Update for Mycobacteria, Showcases Workflow Optimization tools like MALDI Biotyper Pilot™, MALDI ...
Utility for proteomics designed to support the preprocessing and analysis of MALDI-TOF mass spectrometry data that loads data from mzML, mzXML and CSV files. It allows users to apply baseline correction, normalization, smoothing, peak detection and peak matching.
A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]
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The original MALDESI design was implemented using common organic matrices, similar to those used in MALDI, along with a UV laser. The current MALDESI source employs endogenous water or a thin layer of exogenously deposited ice as the energy-absorbing matrix where O-H symmetric and asymmetric stretching bonds are resonantly excited by a mid-IR ...
For higher specific detection of the SARS-CoV-2 virus, Bruker (BRKR) launches luoroType SARS-CoV-2 plus next-generation 6-plex PCR assay.
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