Recombinant Human Furin Protein, CF

Furin is a member of the proprotein convertase (PC) family, which belongs to the subtilisin superfamily of serine protease (1-3). As a cellular protease, Furin processes a variety of proproteins in secretory pathway compartments by cleaving after Arg-Xaa-Lys/Arg-Arg-like motifs, which usually reside at the end of the pro regions of these proproteins. Examples of the proprotein substrates are growth factors and receptors, extracellular matrix proteins, and other proteases. Furin has an essential role in embryogenesis and homeostasis and is implicated in various pathologies such as cancer, neurodegenerative diseases and anthrax. It is synthesized as a 794 amino acid type I transmembrane protein precursor with a signal peptide (residues 1-24), a pro region (residues 25-107), which play a crucial role in the folding, activation and transport of Furin, and a mature chain (residues 108-794) (1-3). The mature chain consists of the subtilisin-like catalytic domain, a P domain, which is essential for enzyme activity and the modulation of pH and calcium requirements, and a cytoplasmic domain, which controls the localization and sorting of Furin in the trans-Golgi network/endosomal system. The purified recombinant human Furin (residues 108-715) corresponds to the mature enzyme terminated before the transmembrane domain.