Protein chip technology, chiefly antibody-based microarrays, can permit analysis of the expression of numerous proteins with a single experiment, and is of major interest in diagnostic fields of biomedical research. However, current technology is low-throughput, based on time-consuming sample preparation, and generally has poor specificity. Researchers across life sciences find that many antibody companies do not sufficiently characterize their antibodies for their needs. UNC's rapid technology addresses this characterization problem by accurately identifying and quantifying the antibody’s binding targets.
Dr. Christoph Borchers at UNC developed a novel protein chip technology based on standard immobilization techniques and mass spectrometric analysis. Digested proteome samples are absorbed onto immobilized antibodies in a microarray format, followed by MALDI-analysis.
Applications include antibody characterization, namely sequencing of peptides bound to antibodies.
- High-throughput compatible: No protein separation is required and the technique is compatible with automation.
- No restriction in protein class (such as membrane-bound, etc).
- Sensitive and specific: Detection of peptides bound to a single bead, in the fmol range; specific protein levels can be accurately determined in complex mixtures.
- Multiple digestions permit epitope mapping.
- Labeled isotopes permit absolute quantification of bound peptides and can be used for measuring antibody affinity.
- All bound peptides are also quantified and sequenced – determine antibody specificity.
Name: Research Tool Manager