our services

By applying mass spectrometry based proteomics, we can analyse almost any biological sample, including cell lines, tissue, formalin fixed paraffin embedded tissue, bio-fluids, plants, fungi, and more. 

Our main application is quantification of proteins using label free or SILAC based methods, in simple and complex biological samples. ‘Discovery’ type experiments can yield as many as 9,000 proteins, depending on the type of sample. We use a variety of data acquisition modes such as DDA and DIA.

Analysis of samples after Co-IP/pulldown for identification of protein-protein interactions and/or posttranslational modifications. 

Enrichment of phosphopeptides using Immobilised Metal Affinity Chromatography on an automated platform. From 100ug protein we can identify and quantify over 10,000 phosphopeptides.

A powerful mass spectrometry technique for specific and sensitive quantification of proteins and their PTMs. Targeted quantification is suitable for hypothesis driven experiments, where the proteins of interest are already known.

We use our novel glycoproteomics workflow, which includes glycopeptide enrichment, data acquisition and software tools for global analysis of glycoproteins. 

It is most applicable for human and mouse, since it relies on a glycan database. 

Analysis of intact proteins for MW determination

We use the CellSignaling antibody to enrich peptides carrying the GG remenant (after digestion with trypsin). 

We deplete the abundant proteins and then analyze by mass spec based proteomics as usual. 

Anaylsis of crosslinked proteins for identification of interaction sites. 

Enrichment of S-nitrosylated peptides using the SNO-RAC method.