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Recombinant Human GFER Protein (His Tag) (PKSH032412)

All Size Price Qty
50μg $ 198.00
10μg $ 88.00
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For research use only.

Synonyms ALR, Augmenter of liver regeneration, FAD-linked sulfhydryl oxidase ALR, GFER, HERV1, HPO, Hepatopoietin, hERV1
Species Human
Expression Host E.coli
Sequence Met 1-Asp125
Accession P55789-2
Calculated Molecular Weight 17.3 kDa
Observed Molecular Weight 15 kDa
Tag N-His
Bio-activity Not validated for activity
Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution of 50mM Glycine-HCl, 150mM NaCl, pH 2.5.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.
Background GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1/ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.
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