GFER Protein, Rat (His-SUMO)

The GFER protein is a FAD-dependent sulfhydryl oxidase that restores redox-active disulfide bonds in CHCHD4/MIA40, an important partner for protein folding in the mitochondrial intermembrane space.GFER Protein, Rat (His-SUMO) is the recombinant rat-derived GFER protein, expressed by E.coli , with N-His, N-SUMO labeled tag.

GFER, a flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidase, serves as a crucial enzyme in the mitochondrial intermembrane space by facilitating the regeneration of redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding. The intricacy of this process involves the reduced form of CHCHD4/MIA40 transiently forming an intermolecular disulfide bridge with GFER/ERV1. This interaction results in the replenishment of essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 undergoes re-oxidization by donating electrons to cytochrome c or molecular oxygen. Beyond its role in redox regulation, GFER may play a functional role in liver regeneration and spermatogenesis, further highlighting its significance in cellular processes beyond mitochondrial protein folding.

Rat

E. coli

N-His;N-SUMO

Q63042 (M1-D198)

27100  [NCBI]

MAAPSEPAGFPRGSRFSFLPGGAHSEMTDDLVTDARGRGARHRKDNAPAAAPAPKGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRNTWAFLHTLAAYYPDMPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIDRSQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD

Approximately 38.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.