Human Furin, His Tag (FUN-H5221) is expressed from human 293 cells (HEK293). It contains AA Gln 25 - Gly 577 (Accession # AAH12181.1).
Predicted N-terminus: Gln 25
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 61.5 kDa. The protein migrates as 55-66 kDa on a SDS-PAGE gel under reducing (R) condition.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 20 mM Tris, 150 mM NaCl, 1 mM CaCl2, 0.01% Birj-35, pH 9.0. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Furin, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
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.
- (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.
- (5) Pesu M., et al., 2008, Nature 455 (7210): 246–50.
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