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Human Furin Recombinant

Furin

accession:  P09958
   Size A     5ug   $ 160
   Size B      20ug  $550
   Size C      100ug  $ 1950
Domain  : 
Gene  :  FURIN
Catalog no. :  RKP09958

 

Source:

Optimized DNA sequence  encoding peptidase domain of Human Furin (ASP108 - GLU715) including a C-terminal His tag was expressed in HEK293 cells.


 
Molecular weight:

Recombinant human Furin is a protein consisting of 615 amino acid residue subunits,due to glycosylation migrates as an approximately 66kDa protein on reduced SDS-PAGE.


 
Purity:
>95%, as determined by SDS-PAGE and HPLC
 
Biological activity:
The activity was tested by the ability of cleave the fluorogenic peptide substrate GATLA–AMC, and was measured to be >150 pMole/min/ug
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Human Furin is lyophilized  from 0.2 μm filtered PBS solution,  pH7.2 ,  5% Trehalose.

              
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

 
Storage:
Recombinant Furin can be stored in working aliquots at 2° - 8° C for one month, or at -20°C to -70°C for twelve months.

Avoid repeated freeze/thaw cycles.

 
Usage:
This product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

FURIN

Furin is ubiquitously expressed as type I transmembrane protein and is present both in vertebrates and invertebrates. The protein is mainly located in the Golgi and trans-Golgi network but may also circulate through the endosomal system to the cell surface and back to the trans-Golgi network, and it is partially shed as a soluble, truncated enzymatically active enzyme . Furin catalyzes the physiological activation of proforms of receptors, hormones, zymogens, and cell surface proteins . It has a more rigid preference for a basic amino acid in the P2 position than other furin- like PCs, leading to its preferred consensus sequence Arg-Xaa-(Lys/Arg)-Arg↓-Xaa, where bulky hydrophobic residues in P1′ position are unfavorable

Related Publications:
a novel activation mechanism of avian influenza virus h9n2 by FURIN
J. Virol., Feb 2014; 88: 1673 - 1683.
prodomain of the proprotein convertase subtilisin/kexin FURIN (ppFURIN) protects from tumor progression and metastasis
Carcinogenesis, Nov 2013; 10.1093/carcin/bgt345.
FURIN is the primary in vivo convertase of angiopoietin-like 3 and endothelial lipase in hepatocytes
J. Biol. Chem., Sep 2013; 288: 26410 - 26418.
identification of serpin determinants of specificity and selectivity for FURIN inhibition through studies of α1pdx (α1-protease inhibitor portland)-serpin b8 and FURIN active-site loop chimeras
J. Biol. Chem., Jul 2013; 288: 21802 - 21814.
endothelial protease nexin-1 is a novel regulator of a disintegrin and metalloproteinase 17 maturation and endothelial protein c receptor shedding via FURIN inhibition
Arterioscler Thromb Vasc Biol, Jul 2013; 33: 1647 - 1654.




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Antibodies:
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product_icon_8.jpg Human Furin Recombinant
 
 
 
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