FURIN
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 85 % as determined by SDS-PAGE and Coomassie blue staining.
FURIN
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
>90 % as determined by SDS-PAGE.
Restrictions
For Research Use only
Format
Lyophilized
Buffer
Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization.
Stock
-20 °C,-80 °C
Stockage commentaire
Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.
This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. It encodes a type 1 membrane bound protease that is expressed in many tissues, including neuroendocrine, liver, gut, and brain. The encoded protein undergoes an initial autocatalytic processing event in the ER and then sorts to the trans-Golgi network through endosomes where a second autocatalytic event takes place and the catalytic activity is acquired. Like other members of this convertase family, the product of this gene specifically cleaves substrates at single or paired basic residues. Some of its substrates include proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor. It is thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140, and may play a role in tumor progression. Unlike SARS-CoV and other coronaviruses, the spike protein of SARS-CoV-2 is thought to be uniquely cleaved by this protease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2020]
Poids moléculaire
predicted molecular mass of 61.0 kDa after removal of the signal peptide. The apparent molecular mass of FURIN-His is 55-70 kDa due to glycosylation.