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In proteomics, depletion of the most abundant proteins is recommended to reduce sample complexity and identify low-abundance proteins that usually provide more biologically and clinically relevant information. Among the proposed bottom-up strategies, the isolation of a subproteome based on the enrichment of peptides containing less abundant amino acids such as cysteine, histidine, methionine or tryptophan has always been of great interest. Hence, the analysis of histidine containing peptides (His-peptides) from enzymatic digests enables to simplify the peptide mixture while keeping a significant coverage of the proteome accessible to quantification.
This service provides an immobilised metal affinity solid-phase extraction containing Ni(II) coupled on-line to capillary electrophoresis-mass spectrometry (IMA-SPE-CE-MS) method to selectively enrich His-peptides from protein tryptic digests and enhance sensitivity. The on-line enrichment and separation method coupled to MS detection is straightforward and advantageous over off-line pretreatment methods in terms of simplicity, cost-effectiveness and throughput.