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High-Performance Supports for Antibody Processing

WINDOWS into the PROTEOME™

High-performance proteome mining for selective protein isolation and biomarker discovery requires the efficient fractionation of complex protein mixtures. One approach to "drilling deeper" into the proteome is the sequential depletion of the most abundant proteins followed by 2D gel or 1D and "2D" column chromatography. Although these approaches can be combined with various hyphenated mass spectroscopy methods, the end result is frequently some combination of a view into the "next most common" proteins and/or a difficult to reproduce proteome fraction. [1] Clearly the ultimate goal of efficient health-versus-disease biomarker identification or proteome-to-phenotype pathway discovery remains problematic.

A preferred approach will take into account both the breadth and complexity of "proteome space" to create biologically interesting sub-proteome fractions that provide a stable and reproducible "window" into the proteome. Examples of efforts in this area include: selective phospho- or glycoproteome isolation and Activity Based Protein Profiling (ABPP). [2,3,4] However, a more global approach would be to create sub-proteome "windows" that combine fractionation reproducibility with the ability to effectively survey the diversity of the proteome. The key to this approach is to recognize that targeting the diversity of proteome space requires complementary diversity from the fractionation strategy.

RECEPTORS has developed an efficient, combinatorial approach to the construction of affinity supports that can be tailored to complement the diversity of proteome space. Our PROTEOME WINDOWS™ Fractionation Supports are based on molecular recognition focused building blocks that are displayed on an affinity support to produce diverse, sub-proteome fractionation environments that are targeted to the exploration of proteome space.

[1] Whiteaker, et.al., Head-to-Head Comparison of Serum Fractionation Techniques, J. Proteome Res., 6, 828-836 (2007).
[2] Zhou, et.al., A Systematic Approach to the Analysis of Protein Phosphorylation, Nature Biotechnology, 19, 375-378 (2001).
[3] Yang, et.al., Multilectin Affinity Chromatography for Characterization of Multiple Glycoprotein Biomarker Candidates in Serum of Breast Cancer Patients, Clin. Chem., 52, 1897-1905 (2006).
[4] Jessani, N., Cravatt, B.F., The Development and Application of Methods for Activity-Based Protein Profiling, Curr. Opin. Chem. Biol., 8, 54-59 (2004).