Recombinant Human AMID protein
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Recombinant Human AMID protein is a Human Fragment protein, in the 1 to 339 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
AMID, PRG3, AIFM2, Ferroptosis suppressor protein 1, FSP1, Apoptosis-inducing factor homologous mitochondrion-associated inducer of death, p53-responsive gene 3 protein
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human AMID protein (AB164678)
ab164678 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis (PubMed : 31634899, PubMed : 31634900, PubMed : 35922516). At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis (PubMed : 31634899, PubMed : 31634900). Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis (PubMed : 31634899, PubMed : 31634900). This anti-ferroptotic function is independent of cellular glutathione levels (PubMed : 31634899, PubMed : 31634900). Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle : catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms (PubMed : 35922516). Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis (PubMed : 35922516). May play a role in mitochondrial stress signaling (PubMed : 26689472). Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death (PubMed : 26689472). Capable of DNA binding in a non-sequence specific way (PubMed : 15958387).
Sequence similarities
Belongs to the FAD-dependent oxidoreductase family.
Post-translational modifications
N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane.
Subcellular localisation
Mitochondrion membrane
Target data
Product promise
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