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Merck

F2677

Sigma-Aldrich

Furin human

≥2,000 unit/mL, buffered aqueous solution, recombinant, expressed in baculovirus infected Sf9 cells

Synonym(e):

Dibasic-processing enzyme, Furin convertase, PACE, Paired basic amino acid residue-cleaving enzyme

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in baculovirus infected Sf9 cells

Qualitätsniveau

Form

buffered aqueous solution

Mol-Gew.

57 kDa

Konzentration

≥2,000 unit/mL

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−70°C

Angaben zum Gen

human ... FURIN(5045)

Anwendung

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. Wirkung

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.
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.

Einheitendefinition

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.

Physikalische Form

Solution in 10 mM MES, pH 7.0 at 25 °C, 1 mM CaCl2, 50% glycerol.

Angaben zur Herstellung

Isolated from Spodoptera frugiperda (Sf9) cells infected with recombinant baculovirus carrying truncated human furin

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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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
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The Journal of general virology, 95(Pt 9), 1991-2003 (2014-06-13)
The molecular basis for the increased resistance of astrocytes to a non-neuropathogenic strain of West Nile virus (WNV), WNV-MAD78, compared with the neuropathogenic strain WNV-NY remains unclear. Here, we demonstrated that the reduced susceptibility of astrocytes to WNV-MAD78 is due
Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site
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Proceedings of the National Academy of Sciences of the USA, 87, 9378-9382 (1991)
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