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Molecular & Cellular Proteomics 2:262-270, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Jefferson Center for Biomedical Research, Doylestown, Pennsylvania 18901
¶ Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
|| Isis Innovation, Ewert House, Ewert Place, Summertown, Oxford OX2 7SG, United Kingdom
** Daniel Baugh Institute for Functional Genomics/Computational Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107
Patient serum or plasma is frequently monitored for biochemical markers of disease or physiological status. Many of the rapidly evolving technologies of proteome analysis are being used to find additional clinically informative protein markers. The unusually high abundance of albumin in serum can interfere with the resolution and sensitivity of many proteome profiling techniques. We have used monoclonal antibodies against human serum albumin (HSA) to develop an immunoaffinity resin that is effective in the removal of both full-length HSA and many of the HSA fragments present in serum. This resin shows markedly better performance than dye-based resins in terms of both the efficiency and specificity of albumin removal. Immunoglobulins are another class of highly abundant serum protein. When protein G resin is used together with our immunoaffinity resin, Ig proteins and HSA can be removed in a single step. This strategy could be extended to the removal of any protein for which specific antibodies or affinity reagents are available.
To whom correspondence should be addressed: Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Jefferson Center for Biomedical Research, Doylestown, PA 18901. Tel.: 215-489-4946; Fax: 215-489-4920; E-mail: laura.steel{at}jefferson.edu
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