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Documenti fondamentali

F2677

Sigma-Aldrich

Furin human

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

Sinonimo/i:

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

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About This Item

Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Ricombinante

expressed in baculovirus infected Sf9 cells

Livello qualitativo

Forma fisica

buffered aqueous solution

PM

57 kDa

Concentrazione

≥2,000 unit/mL

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... FURIN(5045)

Applicazioni

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.

Azioni biochim/fisiol

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.

Definizione di unità

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.

Stato fisico

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

Nota sulla preparazione

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

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Proteasi TEV

Sigma-Aldrich

T4455

Proteasi TEV

Collagenasi suitable for release of physiologically active rat hepatocytes, Type IV, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid

Sigma-Aldrich

C5138

Collagenasi

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
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
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)
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)
ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding.
Anne-Marie Lund Winther et al.
Journal of lipid research, 62, 100071-100071 (2021-03-28)

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