Recombinant Human Furin Protein, CF

Catalog # Availability Size / Price Qty
1503-SE-010
Recombinant Human Furin Protein, CF Enzyme Activity
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Product Details
Citations (7)
FAQs
Supplemental Products
Reviews (1)

Recombinant Human Furin Protein, CF Summary

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
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
Analysis
Asp108 & Asp131
Structure / Form
Mature
Predicted Molecular Mass
67 kDa
SDS-PAGE
58-85 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

1503-SE

Formulation Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl, Brij-35 and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Assay Procedure

Materials
  • 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

























Data Image

Enzyme Activity View Larger

Recombinant Human Furin (1503-SE) is measured by its ability to cleave the fluorogenic peptide substrate pERTKR-AMC (ES013).

Reconstitution Calculator

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Background: Furin

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.

References
  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.
Entrez Gene IDs
5045 (Human); 18550 (Mouse)
Alternate Names
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

Citations for Recombinant Human Furin Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

7 Citations: Showing 1 - 7
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  1. N-Glycosylation is required for secretion of the precursor to brain-derived neurotrophic factor (proBDNF) carrying sulfated LacdiNAc structures
    Authors: J Benicky, M Sanda, Z Brnakova K, R Goldman
    J. Biol. Chem., 2019;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Protein Isolation
  2. c-Met-mediated endothelial plasticity drives aberrant vascularization and chemoresistance in glioblastoma
    Authors: 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
    J Clin Invest, 2016;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  3. A Selective Irreversible Inhibitor of Furin Does Not Prevent Pseudomonas Aeruginosa Exotoxin A-Induced Airway Epithelial Cytotoxicity
    PLoS ONE, 2016;11(7):e0159868.
    Species: Human
    Sample Types: Protein
    Applications: Enzyme Assay
  4. 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
    Authors: Michael Koutsilier
    Growth Horm. IGF Res., 2016;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells.
    Authors: Haage A, Schneider I
    FASEB J, 2014;28(8):3589-99.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Enzyme Assay
  6. Development and characterisation of an assay for furin activity.
    Authors: Bourne GL, Grainger DJ
    J. Immunol. Methods, 2011;364(1):101-8.
    Species: N/A
    Sample Types: N/A
    Applications: ELISA (Standard)
  7. Astacin proteases cleave dentin sialophosphoprotein (Dspp) to generate dentin phosphoprotein (Dpp).
    Authors: Tsuchiya S, Simmer JP, Hu JC, Richardson AS, Yamakoshi F, Yamakoshi Y
    J. Bone Miner. Res., 2010;26(0):220.
    Species: Human
    Sample Types:
    Applications: Bioassay

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Recombinant Human Furin Protein, CF
By Anonymous on 04/17/2020
Application: In vivo study