Furin Recombinant Protein Cat. No.: 96-331

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psi-iconSpecifications
SPECIES:Human
SOURCE SPECIES:HEK293 cells
SEQUENCE:Asp 108 - Glu 715
FUSION TAG:His Tag
TESTED APPLICATIONS:WB
APPLICATIONS:This recombinant protein can be used for WB. For research use only.
BIOLOGICAL ACTIVITY: Measured by its ability to cleave the fluorogenic peptide substrate p – Glu – Arg – Thr – Lys – Arg – AMC. The bioactivity was measured in 100μL reaction mixture containing 4 μg/mL of rhFurin, 50μM substrate, 25 mM Tris, 1 mM CaCl2, 0. 5% (w/v) Brij­35, pH 9. 0. The specific activity is >130 pmol/min/μg.
psi-iconProperties
PURITY:>95% as determined by SDS-PAGE.
PREDICTED MOLECULAR WEIGHT:66.5 kDa
PHYSICAL STATE:Lyophilized
BUFFER:20 mM Tris, 150 mM NaCl, 1 mM CaCl2, 0.01% Birj-35, pH 9.0
STORAGE CONDITIONS:Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles.
psi-iconAdditional Info
ALTERNATE NAMES:FURIN, FUR, PACE, PCSK3, SPC1
ACCESSION NO.:AAH12181.1
OFFICIAL SYMBOL:FURIN
GENE ID:5045
psi-iconBackground and References
BACKGROUND:Furin is also known as paired basic Amino acid Cleaving Enzyme (PACE), is an enzyme which belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. Furin is enriched in the Golgi apparatus, where it functions to cleave other proteins into their mature/active forms. The expression of furin in T-cells is required for maintenance of peripheral immune tolerance. Furin cleaves proteins just downstream of a basic amino acid target sequence (canonically, Arg-X-(Arg/Lys) -Arg'). PACE is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. In addition to processing cellular precursor proteins, furin is also utilized by a number of pathogens. For example, the envelope proteins of viruses such as HIV, influenza and dengue fever viruses must be cleaved by furin or furin-like proteases to become fully functional. PACE also play a role in tumor progression.
REFERENCES:1) Wise RJ., et al., 1991, Proc Natl Acad Sci U S A 87 (23): 9378–82.
2) Kiefer MC., et al., 1992, DNA Cell Biol 10 (10): 757–69.
3) Hallenberger S., et al., 1992, Nature 360 (6402): 358–61.
4) Thomas G., 2002, Nat. Rev. Mol. Cell Biol. 3 (10): 753–66.

FOR RESEARCH USE ONLY.

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