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Determine Molecular Interaction Dissociation Constant By Quantitative FRET Assay

技術優勢: Cost-effective and saves time by 92% – eliminates time-consuming hybridization experiments and affinity purification steps (assay can be performed in one step with the presence of protein contaminants) Accurate, reliable and robust – effective at high affinity nanomolar range

*Abstract: Background:

FRET (Fluorescence Resonance Energy Transfer) assay measures binding affinities of proteins to visualize their interaction with one another. SUMOs (Small Ubiquitin-related Modifiers) are post-translational modification proteins that are involved in many cellular processes with a distinguished role in transcription inhibition when attached to other proteins. SUMO signaling pathways in conjunction with pathogenesis are vigorously investigated to discover the underlying etiological causes for disease. Currently, biopharmaceutical companies spend $1B to find suitable drug targets. Knowledge of protein-protein interactions will help expedite the drug discovery stage and develop new therapeutic drugs that are cheaper and more effective.

Brief Description:

UCR Researchers have developed a novel, quantitative version of the FRET assay to determine accurate and simplified dissociation constant measurements. They were able to achieve this methodology with the SUMO protein and its various interactions with other proteins. The new FRET assay produces consistent and comparable results in less than an hour compared to those of traditional methods that take 12 hours for the same experiment.

*Applications

*Principal Investigation: Name: Ling Jiang
Department:

Name: Jiayu Liao
Department:

Name: Zhehao Xiong
Department:

其他: Images

Wikimedia Commons / https://commons.wikimedia.org/wiki/File:PDB_3d71_EBI.png

Tech ID/UC Case
25154/2015-939-0

Related Cases
2015-939-0

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