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Journal Article

A nonredundant human protein chip for antibody screening and serum profiling

MPS-Authors

Lueking,  Angelika
Max Planck Society;

Possling,  Alexandra
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50100

Beveridge,  Allan
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50409

Lehrach,  Hans
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Cahill,  Dolores J.
Max Planck Society;

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Citation

Lueking, A., Possling, A., Huber, O., Beveridge, A., Horn, M., Eickhoff, H., et al. (2003). A nonredundant human protein chip for antibody screening and serum profiling. Molecular & Cellular Proteomics, 2(12), 1342-1349. doi:10.1074/mcp.T300001-MCP200.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8959-1
Abstract
There is burgeoning interest in protein microarrays, but a source of thousands of nonredundant, purified proteins was not previously available. Here we show a glass chip containing 2413 nonredundant purified human fusion proteins on a polymer surface, where densities up to 1600 proteins/cm2 on a microscope slide can be realized. In addition, the polymer coating of the glass slide enables screening of protein interactions under nondenaturing conditions. Such screenings require only 200-µl sample volumes, illustrating their potential for high-throughput applications. Here we demonstrate two applications: the characterization of antibody binding, specificity, and cross-reactivity; and profiling the antibody repertoire in body fluids, such as serum from patients with autoimmune diseases. For the first application, we have incubated these protein chips with anti-RGSHis6, anti-GAPDH, and anti-HSP90ß antibodies. In an initial proof of principle study for the second application, we have screened serum from alopecia and arthritis patients. With analysis of large sample numbers, identification of disease-associated proteins to generate novel diagnostic markers may be possible.