F2677
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
Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
About This Item
Productos recomendados
recombinante
expressed in baculovirus infected Sf9 cells
Nivel de calidad
Formulario
buffered aqueous solution
mol peso
57 kDa
concentración
≥2,000 unit/mL
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... FURIN(5045)
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Definición de unidad
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.
Forma física
Solution in 10 mM MES, pH 7.0 at 25 °C, 1 mM CaCl2, 50% glycerol.
Nota de preparación
Isolated from Spodoptera frugiperda (Sf9) cells infected with recombinant baculovirus carrying truncated human furin
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Elija entre una de las versiones más recientes:
¿Ya tiene este producto?
Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Los clientes también vieron
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
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
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)
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)
Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.
Póngase en contacto con el Servicio técnico