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Merck

F2677

Sigma-Aldrich

Furin human

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

Sinónimos:

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

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About This Item

MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in baculovirus infected Sf9 cells

Quality Level

form

buffered aqueous solution

mol wt

57 kDa

concentration

≥2,000 unit/mL

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... FURIN(5045)

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 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.

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Journal of lipid research, 62, 100071-100071 (2021-03-28)
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)
Katherine L Hussmann et al.
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
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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