Changes in protein expression are typically not cancer-specific.
We're developing technology to evaluate the changes to the structure of the protein biomarker. These structural changes directly relate to cancer mutations. In contrast to looking at gene mutations, our technology provides direct information about the onset or progression of a disease – instead of just your risk of getting it.
SIA: Simple, Elegant, & Robust
The basis of solvent interaction analysis is the separation of proteins with distinct physiochemical properties by a biphasic system. Two distinct immiscible solvent systems arise when polymers and salts are mixed in water.
Separation based on structural change
A sample is first placed in the aqueous two-phase system. The system is agitated and then centrifuged to thoroughly mix and then separate the solutes. All protein isoforms partition unequally between the top and bottom phases based on their structure and interaction with other proteins.
Our SIA technology reports a quantitative ratiometric parameter that is independent of the absolute expression level, called K, which represents the ratio of the biomarker concentration in a customized biphasic solution. The value of K is used as standard cut-off clinical parameters once calibrated against known clinical samples. How do we measure the biomarker concentration in each of the two phases? With a simple conventional technology such as ELISA, which can detect the biomarker – but is incapable of detecting changes to its structure. That is done by SIA.