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F2677

Sigma-Aldrich

Furin human

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

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD03456906
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
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Produit recombinant

expressed in baculovirus infected Sf9 cells

Niveau de qualité

200

Forme

buffered aqueous solution

Poids mol.

57 kDa

Concentration

≥2,000 unit/mL

Numéro d'accès UniProt

P09958

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... FURIN(5045)

Catégories apparentées

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antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

biological source

rabbit

biological source

rabbit

biological source

mouse

biological source

mouse

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

species reactivity

bovine, human, dog, horse, pig, mouse, rat

species reactivity

human

species reactivity

human

species reactivity

human

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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.[1]

Actions biochimiques/physiologiques

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.[2] 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[3][4].

Définition de l'unité

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.

Forme physique

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

Notes préparatoires

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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    Certificats d'analyse (COA)

    Lot/Batch Number
    SLCL7836
    SLCK1392
    SLCF0512
    SLBP4591V
    SLBP1402V

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    H S Oh et al.
    The Journal of investigative dermatology, 110(6), 939-945 (1998-06-10)
    The epidermis is a stratified squamous epithelium composed primarily of keratinocytes that undergo sequential changes in gene expression during differentiation. CCAAT/enhancer binding proteins (C/EBP) are members of the bZIP family of DNA binding proteins/transcription factors. Northern analysis demonstrated that C/EBPalpha
    Matthew J Ruddy et al.
    The Journal of biological chemistry, 279(4), 2559-2567 (2003-11-06)
    Interleukin (IL)-17 is a recently described cytokine involved in the amplification of inflammatory responses and pathologies. A hallmark feature of IL-17 is its ability to induce expression of other cytokines and chemokines. In addition, IL-17 potently synergizes with tumor necrosis

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