Skip to Content
Merck
All Photos(1)

Documents

F2677

Sigma-Aldrich

Furin human

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

Synonym(s):

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

Sign Into View Organizational & Contract Pricing


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)

Related Categories

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service