A Novel Method for Unambiguous, Quantitative Detection of Full-length and Truncated Thioredoxin from Complex Biological Samples

Unmet Need: Thioredoxin (TRX) is an essential protein that acts as antioxidant and can be used as a general marker of many different disease conditions involving oxidative stress. Currently, the level of thioredoxin is detected using ELISA methods. While potentially informative, there may be several problems inherent in this technique as this protein exists in full-length form (TRX) and truncated form (TRX80) in biological samples. TRX80 has additional properties that may promote several processes including chemoattraction, mitogenesis, and inflammation. Many ELISA methods do not measure TRX80, or may potentially be cross-reactive to TRX80 without accounting for this in obtained values. Since these two forms of the protein have been ascribed different functions, it is important to be able to monitor both forms in a highly quantitative way within the same sample.
Value Proposition:

• Novel method to unambiguously and quantitatively distinguish TRX and TRX80 in complex biological samples
• Samples are denatured and fully digested, thereby eliminating issues of protein/protein interactions

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