protein

Frataxin/FXN Protein, Human (His, Myc)

HY-P72266

2 μg;10 μg;50 μg;100 μg

41;100;282;450 USD

Frataxin/FXN Protein, Human (His, Myc)

proteins

E. coli

2 μg;10 μg;50 μg;100 μg

41;100;282;450 USD

Frataxin/FXN protein activates the core iron-sulfur cluster assembly complex and accelerates sulfur transfer for [2Fe-2S] cluster assembly. It plays a key role in the de novo synthesis of clusters, delivering persulfide to the ISCU. Frataxin/FXN Protein, Human (His, Myc) is the recombinant human-derived Frataxin/FXN protein, expressed by E. coli , with C-Myc, N-10*His labeled tag.

Human

Frataxin/FXN protein serves as an activator within the core iron-sulfur cluster (ISC) assembly complex, facilitating persulfide transfer to the scaffolding protein ISCU and participating in [2Fe-2S] cluster assembly. It expedites sulfur transfer from the NFS1 persulfide intermediate to ISCU and small thiols like L-cysteine and glutathione, leading to persulfuration and sulfide release. Frataxin/FXN is integral to the de novo synthesis of a [2Fe-2S] cluster, initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) producing persulfide, which is delivered to ISCU in a FXN-dependent manner. This complex is stabilized by FDX2, providing reducing equivalents for [2Fe-2S] cluster assembly. The cluster is subsequently transferred from ISCU to chaperone proteins, including HSCB, HSPA9, and GLRX5. Frataxin/FXN may play a role in protecting against iron-catalyzed oxidative stress through its ferroxidase activity, particularly in its oligomeric form. It might also function as an iron chaperone, safeguarding the aconitase [4Fe-4S]2+ cluster and promoting enzyme reactivation. Additionally, Frataxin/FXN may act as a high-affinity iron binding partner for FECH, contributing to mitochondrial heme biosynthesis, modulating the RNA-binding activity of ACO1, and potentially influencing cytoplasmic iron-sulfur protein biogenesis, overall impacting oxidative stress resistance and cell survival.

CyaY; FRDA; X25

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

Lyophilized from 0.22 μm filtered solution in PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.