The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Measured by its ability to cleave the fluorogenic peptide substrate p – Glu – Arg – Thr – Lys – Arg – AMC. The bioactivity was measured in 100µL reaction mixture containing 4 µg/ml of rhFurin, 50 µM substrate, 25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij35, pH 9.0.
The specific activity is >130 pmol/min/µg.
< 1.000 Eu/µg
>95% by SDS-PAGE . ab167741 was lyophilized from 0.22 µm filtered solution.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Constituents: MES, Trehalose Note: Typically between 5-10% trehalose is used for freeze drying, and after reconstitution, the trehalose is approximately 3-5%.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
It is recommended to reconstitute the lyophilized protein in sterile deionized water to a final concentration of 200 ug/ml. Solubilize for 30 to 60 minutes at room temperature with occasional gentle mixing. Carrier protein (0.1% HSA or BSA) is strongly recommended for further dilution and long term storage.
Dibasic processing enzyme
FES upstream region
Furin membrane associated receptor protein
Paired basic amino acid residue cleaving enzyme
Paired basic amino acid residue-cleaving enzyme
Proprotein convertase subtilisin/kexin type 3
Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
Seems to be expressed ubiquitously.
Belongs to the peptidase S8 family. Furin subfamily. Contains 1 homo B/P domain.
Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation. Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.
Golgi apparatus > trans-Golgi network membrane. Cell membrane. Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin.