Furin is a recombinant, ubiquitous subtilisin-like proprotein convertase with a minimal cleavage site of Arg-X-X-Arg˅. However, the enzyme prefers the site Arg-X-Lys/Arg-Arg˅.
- It is the major processing enzyme of the secretory pathway and is localized in the trans-golgi network
- Substrates of Furin include blood clotting factors, serum proteins and growth factor receptors such as the insulin-like growth factor receptor
Furin is a ubiquitous subtilisin-like proprotein convertase. It is the major processing enzyme of the secretory pathway and is localized in the trans-golgi network (1,2). Substrates of Furin include blood clotting factors, serum proteins and growth factor receptors such as the insulin-like growth factor receptor (3). The minimal cleavage site is Arg-X-X-Arg'. However, the enzyme prefers the site Arg-X-(Lys/Arg)-Arg'. An additional arginine at the P6 position appears to enhance cleavage (4). Furin is inhibited by EGTA, α1- Antitrypsin Portland (5) and polyarginine compounds (6).
Product SourceIsolated from Spodoptera frugiperda (Sf9) cells infected with recombinant baculovirus carrying truncated human furin (kindly provided by R. Fuller) (3).
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