Product Details
| Alternative Name: | Furin, PACE, Paired basic amino acid residue cleaving enzyme |
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| MW: | ~81kDa. |
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| Source: | Produced in Drosophila melanogaster Schneider 2 cells. Corresponds to aa 108-714 of the human preproenzyme. Does not contain the C-terminal and transmembrane domains. Produced by plasmid transfection expression. |
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| EC: | 3.4.21.75 |
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| UniProt ID: | P09958 |
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| Quantity: | ~50U/vial. One unit is defined as the amount of enzyme that releases 1pmol AMC from Boc-Arg-Val-Arg-Arg-AMC (Prod. No. ALX-260-040) per minute. |
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| Concentration: | 1U/µl |
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| Formulation: | Liquid. In 100mM HEPES, pH 7.5, containing 25% glycerol, 150mM sodium chloride and 1mM calcium dichloride. |
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| Purity: | ≥90% (one major band at ≥83kDa) |
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| Biological Activity: | Cleaves precursor proteins C-terminal to an Arg-X-X-Arg motif. |
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| Specific Activity: | One unit cleaves 24pmol (2µg) of protective antigen or 100pmol (2.5µg) of human proendothelin-1 per hour at 30°C in 100mM HEPES, pH 7.6, containing 1mM calcium dichloride, 0.5% Triton X-100 and 1mM 2-mercaptoethanol. |
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| Shipping: | Shipped on Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Do not aliquot. Keep vial on ice during use and put immediately back in -80°C freezer. |
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| Handling: | Do not freeze/thaw. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Internally quenched fluorogenic substrate for furin: H. Angliker, et al.; Anal. Biochem.
224, 409 (1995),
Abstract;
Processing of proendothelin-1 by human furin convertase: J.-B. Denault, et al.; FEBS Lett.
362, 276 (1995),
Abstract;
Purification of recombinant soluble forms of furin produced in Chinese hamster ovary cells: K. Nakayama; Meth. Enzymol.
244, 167 (1994),
Abstract;
Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage: R. Leduc, et al.; J. Biol. Chem.
267, 14304 (1992),
Abstract;
Full Text
Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen: S.S. Molloy, et al.; J. Biol. Chem.
267, 16396 (1992),
Abstract;
Full Text
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