ProFACT offers a comprehensive suite of molecular profiling technologies readily integrated with other "omics" data for biomarker and drug target discovery. These include: SeraFILE™, for reduction of protein complexity and sub-proteome creation; Rational Proteome Prospecting™, to enrich and isolate functional activity; Conformerics™, to generate drug screening assays based on enzyme sub-states or conformers; and Rational Genome to Proteome Prospecting™, for prospecting into protein expression based on gene expression data.
In addition to the information contained on this website, these application specific documents can be downloaded by clicking the title:
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.
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.
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.