Furin human

Description

• Application: Furin is capable of cleaving precursors of a wide variety of proteins, including growth factors, serum proteins, including proteases of the blood-clotting and complement systems, matrix metalloproteinases, receptors, viral-envelope glycoproteins, and bacterial exotoxins, typically at sites marked by the consensus sequence Arg-Xaa-(Lys/Arg)-Arg.[1]
• Biochem/physiol Actions: Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It has a molecular mass of 52.7 kDa. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells.[2] Furin cleaves precursor proteins at their paired basic amino acid processing sites. Some substrates of furin include von Willebrand factor, transforming growth factor beta 1 precursor, pro-beta-secretase and proparathyroid hormone[3][4].
• Unit Definition: One unit is defined as the amount of enzyme required to cleave 25 μg of a MBP-FN-paramyosin-ΔSal substrate to 95% completion in 6 hours at 25°C in a total reaction volume of 25 μl.
• Physical form: Solution in 10 mM MES, pH 7.0 at 25 °C, 1 mM CaCl2, 50% glycerol.
• Preparation Note: Isolated from Spodoptera frugiperda (Sf9) cells infected with recombinant baculovirus carrying truncated human furin