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Brochure Document Name Description SeraFILE™ -  Proteomic Connections to Function, Small Molecule Modulation, and Gene Expression  General brochure describing the SeraFILE™ separations platform technology and the applications to functional biomarker prospecting and drug development. Published in Dec. 2009.

Posters Document Name Description Molecular Profiling With SeraFILE™: Prospecting for Conformational Variants   Presented at Cambridge Healthtech ADAPT Conference, Washington DC, Sept, 2009 SeraFILE™ – a proprietary, surface-based separations reagent set and associated exploratory protocols - addresses the disconnect between proteomics and functional mechanisms. Clients and collaborators now employ it as a targeted proteomics approach: for low-abundance enrichment, enzymatic activity-state profiling and functional proteomic prospecting. Preliminary data has established that SeraFILE™ can differentiate conformational variants, suggesting even the characterization of sub-unit equilibrium. These are critical data for drug development and not otherwise available with other proteomics methods, e.g., Mass Spec. New Proteonic Subfractionation Surfaces  Poster Publication Prepared for Nature Methods, February 2008. Proteomics is encumbered by complexity, unreliable quantification, low-throughput technologies, and lacks systemic ability to uncover structural and functional isoform changes. Recent attention has attempted to reduce the complexity of protein samples, particularly with serum due to the presence of three major protein regions: Albumin, Transferrin and Immunoglobulin. To address this problem, several products have been introduced that have selective binding properties towards one or more of the high abundance proteins in serum. These work through high affinity interactions, most notably using immuno-affinity.

Technical Notes Document Name Description Molecular Profiling with SeraFILETM  Poster Publication Prepared for Nature Methods, February 2008. Abstract: The high throughput SeraFILE™ protocol generates biologically active sub-proteome pools with a lesser degree of complexity than the parent protein sample. Thus, dissecting the proteome prior to downstream analyses allows researchers to profile and study proteins in new ways. ProFACT's SeraFILE™ surface library affords high-resolution partitioning of complex protein extracts into differential sub-proteomes that can be further characterized using a variety of downstream applications. Collectively, SeraFILE™-derived protein profiles offer a more comprehensive signature of the starting sample. SeraFILE™ can fractionate proteins and thus signatures may reveal discrete differences in low abundance proteins across samples. It is important to note that no high abundance proteins are removed from the sample prior to fractionation; they are distributed across sub-proteomes. Therefore, SeraFILE™ facilitates detection of disease-specific differences in clinical proteomics applications. Reproducibility Of SeraFILE™ Derived Functional Proteomic Profiles Prepared as an Application Report, April 2007. Abstract: As sample heterogeneity causes normalization problems when characterizing across multiple samples, we describe here a validation of SeraFILE™ derived profile reproducibility within a broad protein variance window. In serum studies, it was experimentally determined that the amount of total protein can vary by up to 4X, while enzymatic activity profile patterns are consistently observed. This may be useful in tumor studies for example, where relative differences can still be interpreted, despite any disparities in the starting total tissue weight and/or total protein analyzed. In addition, since protein and enzymatic activity profiles are reproducible over a range of protein application concentrations, the profiles may be used as predictors of sub-proteomes containing the highest enrichment of functional activities. Such predictive information may be useful for further prospecting and purification. Functional Proteomics Signature Of The Ubiquitin / Proteasome Pathway   Prepared as an Application Report, March 2007. This report presents preliminary findings on the application of ProFACT's surface library - SeraFILE™, to the functional proteomic characterization of an important cellular pathway, the Ubiquitin/ Proteasome pathway (UPP). The results show: Markedly contrasted signatures of matched cancer to normal adjacent tissue, Differential pools of Proteasome regions and regulatory factors, Altered catalytic rates, both higher and lower, on several different surfaces, Evidence of conformational variants resistant to small molecule inhibitors, Evidence of soluble regulatory factors that potentially could be isolated.