Recombinant Human Furin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human 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 >125 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human Furin protein
Asp108-Glu715, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Asp108 & Asp131
Structure / Form
Mature
Protein/Peptide Type
Recombinant Enzymes
Gene
FURIN
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
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.
SDS-PAGE
65-85 kDa, reducing conditions
Publications
Read Publications using
1503-SE in the following applications:

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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Assay Procedure
  • Assay Buffer:  25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij-35, pH 9.0
  • Recombinant Human Furin (rhFurin) (Catalog # 1503-SE)
  • Substrate: p-Glu-Arg-Thr-Lys-Arg-AMC (Catalog # ES013)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhFurin to 4 µg/mL in Assay Buffer.
  2. Dilute Substrate to 100 µM in Assay Buffer.
  3. 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.
  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:
  • rhFurin: 0.2 µg
  • Substrate: 50 µM

Notes

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

Alternate Names for Recombinant Human 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 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.

  1. Van den Ouweland, A.M. et al. (1990) Nucleic Acids Res. 18:664.
  2. Barr, P.J. et al. (1991) DNA Cell Biol. 10:319.
  3. Thomas, G. (2002) Nature Rev. Mol. Cell Biol. 3:753.

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Publications for Furin (1503-SE)(6)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 3 applications: Bioassay, ELISA (Standard), Enzyme Assay.


Filter By Application
Bioassay
(2)
ELISA (Standard)
(1)
Enzyme Assay
(3)
All Applications
Filter By Species
Human
(5)
N/A
(1)
All Species
Showing Publications 1 - 6 of 6.
Publications using 1503-SE Applications Species
Michael Koutsilier Identification of the IGF-1 processing product human Ec/rodent Eb peptide in various tissues: Evidence for its differential regulation after exercise-induced muscle damage in humans Growth Horm. IGF Res., 2016;0(0):. 2016 [PMID: 27836414] (Bioassay, Human) Bioassay Human
A Selective Irreversible Inhibitor of Furin Does Not Prevent Pseudomonas Aeruginosa Exotoxin A-Induced Airway Epithelial Cytotoxicity PLoS ONE, 2016;11(7):e0159868. 2016 [PMID: 27459298] (Enzyme Assay, Human) Enzyme Assay Human
M Huang, T Liu, P Ma, RA Mitteer, Z Zhang, HJ Kim, E Yeo, D Zhang, P Cai, C Li, L Zhang, B Zhao, L Roccogrand, DM O'Rourke, N Dahmane, Y Gong, C Koumenis, Y Fan c-Met-mediated endothelial plasticity drives aberrant vascularization and chemoresistance in glioblastoma J Clin Invest, 2016;0(0):. 2016 [PMID: 27043280] (Enzyme Assay, Human) Enzyme Assay Human
Haage A, Schneider I Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells. FASEB J, 2014;28(8):3589-99. 2014 [PMID: 24784579] (Enzyme Assay, Human) Enzyme Assay Human
Bourne GL, Grainger DJ Development and characterisation of an assay for furin activity. J. Immunol. Methods, 2011;364(1):101-8. 2011 [PMID: 21112328] (ELISA (Standard), N/A) ELISA (Standard) N/A
Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp). J. Bone Miner. Res., 2010;26(0):220. 2010 [PMID: 20687161] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol FURIN
Uniprot