Recombinant Human Furin His-tag Protein, CF Summary
Product Specifications
Asp108-Ala574, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
11338-SE
| Formulation | Supplied as a 0.2 μm filtered solution in Tris, CaCl2, NaCl, Brij-35 and Glycerol. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Assay Procedure
- Assay Buffer: 25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij-35, pH 9.0
- Recombinant Human Furin (rhFurin) (Catalog # 11338-SE)
- Substrate: p-Glu-Arg-Thr-Lys-Arg-AMC (Catalog # ES013), 8 mM stock in DMSO
- Black 96-well Plate
- Plate Reader with Fluorescence Read Capability
- Dilute rhFurin to 4 µg/mL in Assay Buffer.
- Dilute Substrate to 100 µM in Assay Buffer.
- Load into a black 96-well plate 50 µL of 4 µg/mL 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 plate 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) |
- rhFurin: 0.2 µg
- Substrate: 50 µM
Scientific Data
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Recombinant Human Furin (Catalog # 11338-SE) is measured by its ability to cleave the fluorogenic peptide substrate pERTKR-AMC (ES013).
Reconstitution Calculator
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 cleaves after Arg-Xaa-Lys/Arg-Arg-like motifs typically at the end of the pro region in a variety of proproteins within the secretory pathway including growth factors and receptors, extracellular matrix proteins, and other proteases. Through regulation of proprotein maturation, Furin has an essential role in embryogenesis and homeostasis and is implicated in various pathologies such as cancer (4), neurodegenerative diseases (5) and infectious disease (6). Furin 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) that plays 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 corresponds to a truncated form of 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.
- He, Z. et al. (2022) Oncogene. 9:1252.
- Zhang, Y. et al. (2022) Transl. Neurodegener. 11:39.
- Braun, E. and D. Sauter (2019) Clin. Transl. Immunology. 8:e1073.
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