Proteome Mapping is a technique in which the proteome is analysed by LCMS: a combination of chromatography separation and mass spectrometry.
Pure protein sample is digested and run through an extended 1- or 2-D LC gradient, and the eluent injected into a LCMS instrument. MS spectra are analysed to identify proteins of interest.
Outcomes of this protein analysis are dependent on the quantity and range of proteins present. A 1D LC-MS/MS analysis will identify >1000 proteins. If the sample is complex (e.g whole cell lysate) a more sophisticated 2D LC-MS/MS protocol is used. The sample is first separated by strong cation exchanged chromatography, followed by reverse-phase chromatography and analysed by 2D LC-MS/MS which can identify >2000 proteins in one experiment.
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For more information please refer to PI publications:
1D LC: 20μg of pure protein.
2D LC: 100-200μg of pure protein; however if sample requires additional cleanup we recommend 200-500μg.
Essentially any protein sample such as cell lysate, whole tissue, secreted proteins, but not radioactive samples.
# Note: secreted samples must be in serum/plasma free media.
The sample volume must be less than 250µL.
Yes, protease inhibitors will minimise protein degradation.
Yes, proteome mapping analysis works best on samples from a known genome. Where genomes are partially known, proteome mapping approach will give limited results. However, Proteomics International’s advanced de novo sequencing techniques can be applied.
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