GRADE & PURITYBioactive?Bioactive grade — verified to retain biological activity in functional assays. Use when the molecule must be functionally active, not just pure.Recombinant?Recombinant — produced via recombinant expression for defined sequence and consistency. Use for reproducible, animal-free proteins of known origin.ActiBioPure™?ActiBioPure™ — Aladdin's premier line for bioactive and recombinant products. Use when both high purity and preserved biological activity are required.High Performance?High-performance grade with optimized purity and performance characteristics. Use for sensitive analyses where ordinary grades fall short.EnzymoPure™?EnzymoPure™ — Aladdin's line of high-quality enzymatic solutions. Use when enzyme purity and defined activity drive assay or process performance.expressed in Baculovirus-Sf9 Cells,2,000 U/ml
Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,expressed in Baculovirus-Sf9 Cells,2,000 U/ml ActiBioPure™,Bioactive,High Performance,Recombinant,EnzymoPure™ for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
Furin is a ubiquitous subtilisin-like proprotein convertase. It is the major processing enzyme of the secretory pathway and is localized in the trans-golgi network. Substrates of Furin include blood clotting factors, serum proteins and growth factor receptors such as the insulin-like growth factor receptor. The minimal cleavage site is Arg-X-X-Arg'. However, the enzyme prefers the site Arg-X-(Lys/Arg)-Arg'. An additional arginine at the P6 position appears to enhance cleavage. Furin is inhibited by EGTA, α1- Antitrypsin Portland and polyarginine compounds.
Source: Isolated from Spodoptera frugiperda (Sf9) cells infected with recombinant baculovirus carrying truncated human furin.
Assay Conditions for Unit Activity
Two fold dilutions of Furin are incubated with 25 µg MBP-FN-paramyosin-ΔSal substrate in 20 mM HEPES, 0.1% Triton X-100, 1 mM CaCl2, 0.2mM β-mercaptoenthanol (pH 7.5 @ 25°C) in a 25 µl reaction. The reaction mix is incubated at 25°C for 6 hours. Separation of reaction products are visualized by SDS-PAGE.
ActiBioPure™, Bioactive, High Performance, Recombinant, EnzymoPure™
Specifications & Purity
Bioactive, Recombinant, ActiBioPure™, High Performance, EnzymoPure™, expressed in Baculovirus-Sf9 Cells, 2, 000 U/ml
Biochemical and Physiological Mechanisms
Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. Converts through proteolytic cleavage the non-functional Brain na
Both Furin and Onchocerca volvulus Blisterase will cleave peptide substrates with the sequence, Arg-X- (Lys/Arg)-Arg. However, the ability of either enzyme to cleave a particular protein substrate depends on its tertiary structure as well as on the amino acids immediately surrounding the cleavage site.
CAS
141760-45-4
Enzyme Commission Number
3.4.21.75
Molecule Type
Enzyme
Storage and Shipping
Concentration
expressed in Baculovirus-Sf9 Cells,2,000 U/ml
Storage
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20℃ long term (12 months). Upon receipt, it is recommended to aliquot. Avoid freeze/thaw cycle.
Unit definition
1 unit is defined as the amount of enzyme required to cleave 25 µg of a MBP-FN-paramyosin-ΔSal substrate to 95% completion in 6 hours at 25°C in a total reaction volume of 25 µl.
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
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