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ActiveMax® Recombinant Human GFER /ALR  pdf  pdf  pdf


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Synonym

GFER,ALR,ERV1,HERV1,HPO,HPO1,HPO2,HSS,Hepatopoietin

Source

Recombinant Human GFER /HPO Protein,HEK293 expressed,ActiveMax (rh GFER) Met 81 - Asp 205 (Accession # NP_005253) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

rh GFER contains no "tag", and has a calculated MW of 15.2 kDa. The predicted N-terminus is Met 81. DTT-reduced Protein migrates as 16 kDa in SDS-PAGE .

Endotoxin

Less than 1.0 EU per μg of the rh GFER by the LAL method.

Purity

>92% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in 20 mM Tris, 100 mM NaCl, pH 8.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

 

SDS-PAGE


Recombinant Human GFER /HPO Protein,HEK293 expressed,ActiveMax
The purity of rh GFER was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 

Background

Growth factor, augmenter of liver regeneration (GFER) is also known as FAD-linked sulfhydryl oxidase ALR, which belongs to the Erv1/ALR family of proteins. This family can be found in higher and lower eukaryotes. There are two isoform of GFER: Isoform 1 and isoform 2. Isoform 2 missing 1 – 80 aa. Isoform 1 is mainly located in mitochondrion intermembrane space, while Isoform 1 is secreted to cytoplasm. Isoform 1 of GFER regenerates 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. The isoform 2 of GFER may act as an autocrine hepatotrophic growth factor promoting liver regeneration.

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References

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