Analytical Data
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Gene name
Fumarylacetoacetase/FAH
- Application
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Alternative Names
FAA; Fumarylacetoacetase; Tyrosinemia 1; Beta-diketonase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P16930
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Expression Region
Val189~Ser419
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Molecular Weight
26kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Fumarylacetoacetase (FAH) is a crucial enzyme in the tyrosine catabolism pathway, playing a vital role in the conversion of fumarylacetoacetate to acetoacetate and fumarate. Deficiency in FAH leads to a rare genetic disorder known as hereditary tyrosinemia type I (HT1), characterized by severe liver dysfunction, renal failure, and neurological complications. The accumulation of toxic metabolites in HT1 patients necessitates the development of effective therapeutic strategies. Research on recombinant FAH has gained significant attention as a potential treatment option. By expressing FAH in various host systems, such as bacteria or mammalian cells, scientists aim to produce functional enzyme that can be used for enzyme replacement therapy (ERT) or in cell-based therapies. Advances in protein engineering and purification techniques have improved the yield and activity of recombinant FAH, making it a promising candidate for clinical applications. Moreover, ongoing studies focus on understanding the enzyme's structure-function relationship, which may provide insights into the design of small molecule drugs or gene therapies that could enhance FAH activity in patients. The successful development of recombinant FAH could significantly improve the quality of life for individuals with HT1 and pave the way for innovative treatments for other metabolic disorders.
