>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
67 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhFurin to 4 µg/mL in Assay Buffer.
Dilute Substrate to 100 µM in Assay Buffer.
Load into a black well plate 50 µL of 4 µg/mL of rhFurin, and start the reaction by adding 50 µL of 100 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 100 µM Substrate.
Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)
*Adjusted for Substrate Blank
**Derived using calibration standard 7-amino, 4-Methyl Coumarin (Sigma, Catalog # A-9891).
rhFurin: 0.2 µg
Substrate: 50 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Furin Protein, CF
Furin is a member of the proprotein convertase (PC) family, which belongs to the subtilisin superfamily of serine protease (1-3). As a cellular protease, Furin processes a variety of proproteins in secretory pathway compartments by cleaving after Arg-Xaa-Lys/Arg-Arg-like motifs, which usually reside at the end of the pro regions of these proproteins. Examples of the proprotein substrates are growth factors and receptors, extracellular matrix proteins, and other proteases. Furin has an essential role in embryogenesis and homeostasis and is implicated in various pathologies such as cancer, neurodegenerative diseases and anthrax. It is synthesized as a 794 amino acid type I transmembrane protein precursor with a signal peptide (residues 1-24), a pro region (residues 25-107), which play a crucial role in the folding, activation and transport of Furin, and a mature chain (residues 108-794) (1-3). The mature chain consists of the subtilisin-like catalytic domain, a P domain, which is essential for enzyme activity and the modulation of pH and calcium requirements, and a cytoplasmic domain, which controls the localization and sorting of Furin in the trans-Golgi network/endosomal system. The purified recombinant human Furin (residues 108-715) corresponds to the mature enzyme terminated before the transmembrane domain.
Van den Ouweland, A.M. et al. (1990) Nucleic Acids Res. 18:664.
Barr, P.J. et al. (1991) DNA Cell Biol. 10:319.
Thomas, G. (2002) Nature Rev. Mol. Cell Biol. 3:753.
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