Recombinant Mouse Furin Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Mouse Furin Protein, CF Summary

Details of Functionality
Measured by its ability to cleave the fluorogenic peptide substrate pERTKR-AMC (Catalog # ES013). The specific activity is >150 pmol/min/μg, as measured under the described conditions.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Furin protein
Gln25-Glu714, with a C-terminal 10‑His tag
Accession #
N-terminal Sequence
Asp108, Cys198, Ser239, Glu684
Protein/Peptide Type
Recombinant Enzymes
Gene
Furin
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
77 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.
SDS-PAGE
60-80 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl, Brij-35 and Glycerol.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.
Assay Procedure
  • Assay Buffer: 25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij-35, pH 9.0
  • Recombinant Mouse Furin (rmFurin) (Catalog # 6450-SE)
  • Substrate: p-Glu-Arg-Thr-Lys-Arg-AMC (Catalog # ES013), 8 mM in deionized water
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: Gemini EM by Molecular Devices) or equivalent
  1. Dilute rmFurin to 2 μg/mL in Assay Buffer.
  2. Dilute Substrate to 100 µM in Assay Buffer.
  3. Load into a black well plate 50 µL of the 2 μg/mL rmFurin and start the reaction by adding 50 µL of 100 µM substrate.
  4. Read at excitation and emission wavelengths of 380 nm and 460 nM (top read), respectively, in kinetic mode for 5 minutes.
  5. 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).

Per Well:
  • rmFurin: 0.1 µg
  • Substrate: 50 µM

Notes

Coomassie is a registered trademark of Imperial Chemical Industries Ltd.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Furin Protein, CF

  • Dibasic-processing enzyme
  • EC 3.4.21
  • EC 3.4.21.75
  • FUR
  • FURdibasic processing enzyme
  • furin (paired basic amino acid cleaving enzyme)
  • Furin
  • furin, membrane associated receptor protein
  • PACE
  • PACEFES upstream region
  • paired basic amino acid cleaving enzyme (furin, membrane associated receptorprotein)
  • Paired basic amino acid residue-cleaving enzyme
  • PC
  • PCSK3
  • PCSK3furin
  • proprotein convertase subtilisin/kexin type 3
  • SPC1

Background

Furin is a member of the proprotein convertase (PC) family, which belongs to the subtilisin superfamily of serine proteases. 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 (1, 2). Mouse Furin is a 793 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 108‑793) (2, 3). Mouse Furin displays ~94% homology to the human Furin sequence and >99% homology to the subtilisin‑like catalytic domain (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 (1). The purified recombinant mouse Furin (residues 108‑714) corresponds to the mature enzyme terminated before the transmembrane domain.
  1. Thomas, G. (2002) Nature Rev. Mol. Cell Biol. 3:753.
  2. Creemers, J.W. and W.J. Van de Ven. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.), pp. 1531, Academic Press, San Diego.
  3. Hatsuzawa, K. et al. (1990) J. Biol. Chem. 265:22075.

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Bioinformatics

Gene Symbol Furin
Uniprot