Human Furin / PCSK3 Protein, His Tag

Source : 

Human Furin, His Tag (FUN-H5221) is expressed from human 293 cells (HEK293). It contains AA Gln 25 - Gly 577 (Accession # AAH12181.1).

 

Molecule : Furin

 

Synonyms : FURIN,FUR,PACE,PCSK3,SPC1

 

Format : Powder

 

Category : Enzymes

 

Accession : AAH12181.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 61.5 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 61.5 kDa. The protein migrates as 60-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : 20 mM Tris, 150 mM NaCl, 1 mM CaCl2, pH9.0

 

Description :

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.
(5) Pesu M., et al., 2008, Nature 455 (7210): 246–50.