F2677
Furin human
≥2,000 unit/mL, buffered aqueous solution, recombinant, expressed in baculovirus infected Sf9 cells
Synonyme(s) :
Dibasic-processing enzyme, Furin convertase, PACE, Paired basic amino acid residue-cleaving enzyme
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Furin human, ≥2,000 unit/mL, buffered aqueous solution, recombinant, expressed in baculovirus infected Sf9 cells
recombinant
expressed in baculovirus infected Sf9 cells
form
buffered aqueous solution
mol wt
57 kDa
concentration
≥2,000 unit/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... FURIN(5045)
Catégories apparentées
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.
Biochem/physiol Actions
Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells.
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. 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.
Other Notes
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
Classe de stockage
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15
M.C. Kiefer et al.
Dna and Cell Biology, 10, 757-769 (1992)
Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site
R.J. Wise et al.
Proceedings of the National Academy of Sciences of the USA, 87, 9378-9382 (1991)
D A Bravo et al.
The Journal of biological chemistry, 269(41), 25830-25837 (1994-10-14)
Maturation of the insulin proreceptor in a late Golgi compartment requires cleavage at an Arg-Lys-Arg-Arg processing site, suggesting involvement of furin, a transmembrane serine protease of the Kex2 family of processing enzymes. A genetically engineered secreted, soluble form of human
Jae-Wan Jung et al.
Plant biotechnology journal, 20(7), 1363-1372 (2022-03-25)
We have investigated the use of transient expression to produce virus-like particles (VLPs) of severe acute respiratory syndrome coronavirus 2, the causative agent of COVID-19, in Nicotiana benthamiana. Expression of a native form of the spike (S) protein, either alone
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