The Recombinant Human GFER/ALR Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating GFER/ALR function and its implications in health and disease.
This product (SKU: RPCB1769) is produced using E. coli and features a N-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 17.3 kDa with an observed molecular weight of 15 kDa under denaturing conditions, achieving ≥ 90 % as determined by SDS-PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human GFER/ALR Protein (RPCB1769), tested reactivity in E. coli and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 1 EU/μg of the protein by LAL method.
Purity:
≥ 90 % as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.Contact us for customized product form or formulation.
Reconstitution:
Centrifuge the tube before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
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.
Recombinant Human GFER/ALR Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
