FAH Recombinant Rabbit mAb (S-5082-7)

FAH (fumarylacetoacetate hydrolase) is a metabolic enzyme encoded by the FAH gene on human chromosome 15, mainly expressed in the liver, and is a key enzyme in the catabolic pathway of phenylalanine and tyrosine, catalyzing the hydrolytic cleavage of the carbon–carbon bond of fumarylacetoacetate to yield fumarate and acetoacetate. The enzyme exists as a homodimer, and its active site contains Ca²⁺; its catalytic mechanism involves the metal ion, a Glu/His catalytic dyad, and a charged oxyanion hole. Deficiency of the FAH gene leads to the toxic accumulation of fumarylacetoacetate and its metabolic derivative succinylacetone, causing the human autosomal recessive disease tyrosinemia type I, which is associated with hepatic and renal abnormalities and neurological impairment; patients experience continuous hepatocyte injury and carry an extremely high risk of hepatocellular carcinoma. Notably, recent studies have also found that FAH is upregulated in glioblastoma and promotes tumor progression by activating the PI3K/AKT/mTOR signaling pathway, suggesting that, in addition to its metabolic function, it may have potential pro-oncogenic effects.