Furin Recombinant Protein

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa- (K/R) -R, where Xaa can be any amino acid. Recombinant human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor plus a C-terminal His tag.

The lyophilized Furin recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted Furin stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing Furin recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.