Investigation of the mouse serum proteome

Brian L. Hood, Ming Zhou, King C. Chan, David A. Lucas, Grace J. Kim, Haleem J. Issaq, Timothy D. Veenstra, Thomas P. Conrads*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

56 Scopus citations


With the rapid assimilation of genomic information and the equally impressive developments in the field of proteomics, there is an unprecedented interest in biomarker discovery. Although human biofluids represent increasingly attractive samples from which new and more accurate disease biomarkers may be found, the intrinsic person-to-person variability in these samples complicates their discovery. One of the most extensively used animal models for studying human disease is mouse because, unlike humans, they represent a highly controllable experimental model system. Unfortunately, very little is known about the proteomic composition of mouse serum. In this study, a multidimensional fractionation approach on both the protein and the peptide level that does not require depletion of highly abundant serum proteins was combined with tandem mass spectrometry to characterize proteins within mouse serum. Over 12 300 unique peptides that originate from 4567 unique proteins-approximately 16% of all known mouse proteins-were identified. The results presented here represent the broadest proteome coverage in mouse serum and provide a foundation from which quantitative comparisons can be made in this important animal model.

Original languageEnglish
Pages (from-to)1561-1568
Number of pages8
JournalJournal of Proteome Research
Issue number5
StatePublished - Sep 2005
Externally publishedYes


  • Mouse
  • Multidimensional fractionation
  • Serum proteomics
  • Tandem mass spectrometry


Dive into the research topics of 'Investigation of the mouse serum proteome'. Together they form a unique fingerprint.

Cite this