Furin, Recombinant Mouse

Furin is a member of the proprotein convertase (PC) family, which belongs to the subtilisin superfamily of serine proteases. As a cellular protease, Furin processes a variety of proproteins in secretory pathway compartments by cleaving after ArgXaaLys/ArgArglike 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 (1, 2). Mouse Furin is a 793 amino acid type I transmembrane protein precursor with a signal peptide (residues 1 24), a pro region\n(residues 25 107), which play a crucial role in the folding, activation and transport of Furin, and a mature chain (residues 108 793) (2, 3). Mouse Furin displays ~94% homology to the human Furin sequence and >99% homology to the subtilisinlike catalytic domain (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 transGolgi network/endosomal system (1). The purified recombinant mouse Furin (residues 108 714) corresponds to the mature enzyme terminated before the transmembrane domain. \n\nSource: \nRecombinant corresponding to Gln25-Glu714 from mouse Furin, N-terminal human CD33 signal peptide and a C-terminal, 10-His tag, expressed in CHO cells.\n\nMolecular Weight: \n~77kD\n\nBiological Activity:\nMeasured by its ability to cleave the fluorogenic peptide substrate pERTKR-AMC, The specific activity is >150 pmoles/min/ug, as measured under the described conditions.\n\nEndotoxin Level:\n<1EU/ug (LAL method)\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

F9201-20

Size

10ug

Form

Supplied as a liquid in Tris, Calcium Chloride2, sodium chloride, Brij-35, Glycerol.

Purity

~95% (SDS-PAGE)

References

1. Thomas, G. (2002) Nature Rev. Mol. Cell Biol. 3:753. 2. Creemers, J.W. and W.J. Van de Ven. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.), pp. 1531, Academic Press, San Diego. 3. Hatsuzawa, K. et al. (1990) J. Biol. Chem. 265:22075.