size : | Price | Quantity | |
---|---|---|---|
5 mg | $50.00 | ||
25 mg | $130.00 |
PR-619 (2645-32-1) is a nonselective, reversible inhibitor of cysteine-reactive deubiquitinating enzymes (DUBs; 5-20 μM)1. PR-619 is highly useful for preserving ubiquitinated proteins during cell lysis. DUBs become unregulated in cell lysates and will act quickly to deubiquitinate proteins of interest during cell lysis. To preserve maximum amounts of ubiquitinated protein, include PR-619 (50-100 μM) in lysis buffers. PR-619 is also useful for interrogating the role of DUBs in intact cell systems2, and treatment of cells results in an overall accumulation of ubiquitinated proteins and many other phenotypes.
References/Citations:
1) Altun et al. (2011), Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes; Chem. Biol., 18 1401
2) Seiberlich et al. (2012), The small molecule inhibitor PR-619 of deubiquitinating enzymes affects the microtubule network and causes protein aggregate formation in neural cells: implications for neurodegenerative diseases; Biochim. Biophys. Acta, 1823 2057
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PR-619 (2645-32-1) is a nonselective, reversible inhibitor of cysteine-reactive deubiquitinating enzymes (DUBs; 5-20 μM)1. PR-619 is highly useful for preserving ubiquitinated proteins during cell lysis. DUBs become unregulated in cell lysates and will act quickly to deubiquitinate proteins of interest during cell lysis. To preserve maximum amounts of ubiquitinated protein, include PR-619 (50-100 μM) in lysis buffers. PR-619 is also useful for interrogating the role of DUBs in intact cell systems2, and treatment of cells results in an overall accumulation of ubiquitinated proteins and many other phenotypes.
References/Citations:
1) Altun et al. (2011), Activity-based chemical proteomics accelerates inhibitor development for deubiquitylating enzymes; Chem. Biol., 18 1401
2) Seiberlich et al. (2012), The small molecule inhibitor PR-619 of deubiquitinating enzymes affects the microtubule network and causes protein aggregate formation in neural cells: implications for neurodegenerative diseases; Biochim. Biophys. Acta, 1823 2057
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