Proteome Mapping

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:


Frequently Asked Questions

What amount of protein is required?

1D LC: 20μg of pure protein.
2D LC: 100-200μg of pure protein; however if sample requires additional cleanup we recommend 200-500μg.

What type of sample can be analysed?

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.

What is the maximum volume of sample?

The sample volume must be less than 250µL.

Can I use protease inhibitors?

Yes, protease inhibitors will minimise protein degradation.

Is it important that the proteome you are looking at is in currently available databases?

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.

Please contact us on for a quote.


Please refer to our FAQ brochure for more details.


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