The latest in Proteomics research and news

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The latest in Proteomics research and news

Application Note 471: Analysis of Sialylated Glycans with the MALDI
LTQ Orbitrap Mass Spectrometer using DHB/N,N-Dimethylaniline Matrix

Alterations in glycan structures can have great biological
significance. Of particular interest are sialylated glycans due to
their involvement in processes such as cell-cell adhesion and
cell-pathogen interaction. Thermo Fisher Scientific has developed a
fast, simple, and reliable workflow for profiling N-linked glycans. It
combines the benefits of the Thermo Scientific MALDI LTQ Orbitrap mass
spectrometer with the homogeneity of sample distribution provided by a
DHB/DMA matrix. The high mass accuracy and mass resolution provided by
the Orbitrap™ detector enables confident structural discrimination
without the aid of tandem MS. The ability to profile both sialylated
and asialylated glycans with a single ionization mode in MALDI
experiments makes the workflow is especially useful in determining the
degree of silaylation relative to overall glycan composition.

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