分子量:66.5 kDa

纯度:>95% as determined by SDS-PAGE.

内毒素:Less than 1.0 EU per μg of the Human Furin, His Tag by the LAL method.

Buffer:MES,  Brij-35

生物活性: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 g/mL of rhFurin, 50 μM substrate, 25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij35, pH 9.0. The specific activity is >130 pmol/min/g.

产品特性:Human Furin, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 66.5 kDa. The predicted N-terminus is Asp 108. The reducing (R) protein migrates as 55-66 kDa in SDS-PAGE .

产品背景: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.