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LI-COR Introduces Three IRDye(R) Near-Infrared Fluorescence Resonance Energy Transfer (NIR-FRET) Protease Substrates
Date:11/12/2008

LINCOLN, Neb., Nov. 12 /PRNewswire/ -- Protease substrates provide a sensitive method to detect protease activity, measure potency of inhibitors and screen compound collections for discovery of drug candidates. LI-COR Biosciences now offers three different IRDye NIR-FRET Protease Substrates: IRDye 800CW/QC-1 HIV-1, IRDye 800CW/QC-1 BACE, and IRDye 800CW/QC-1 CSP-3.

"These substrates have low intrinsic fluorescence due to self-quenching of the conjugated dye by our novel IRDye QC-1 quencher," says Jim Wiley, LI-COR strategic marketing manager. "These new substrates can be used for the highly sensitive detection of protease activity via near-infrared fluorescence detection on the Odyssey(R) Infrared Imaging System, Aerius(R) Automated Imaging System, or other imaging systems with near infrared detection capabilities."

"NIR detection dramatically reduces background, scattering and interference from other compounds," says Wiley. He notes that all three substrates have excellent water solubility.

HIV-1 protease performs an essential step in the life cycle of HIV virus by cleaving Gag and Gas-Pol polyproteins into the constituent proteins that make up infectious virus particles. Anti-AIDS drugs targeting HIV-1 protease substantially suppress HIV viral replication and dramatically reduce mortality among HIV infected patients.

Beta-Secretase (BACE-1) has been identified as a key enzyme that mediates a critical step in the formation of Beta-amyloid (ABeta40/42) by acting upon the Beta-amyloid precursor protein (Beta-APP). Deposits of Beta-amyloid form plaques in the brain that lead to damage and death of nerve cells. Plaques are one of the abnormal structures that are characteristic of Alzheimer's disease. Since the discovery of the function of Beta-Secretase, it has been established as a validated therapeutic target for Alzheimer's disease.

Caspases are a family of intracellular cysteine proteases that are vital in the process of ap
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SOURCE LI-COR Biosciences
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