Analytical Data
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Gene name
Fumarate hydratase/FH
- Application
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Alternative Names
FH; Fumarate Hydratase, mitochondrial
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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
P07954#
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Expression Region
Ala45~Asn188
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Molecular Weight
20kDa
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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
Related Products
Protein Description
Fumarate hydratase (FH) is a crucial enzyme involved in the tricarboxylic acid (TCA) cycle, catalyzing the reversible hydration of fumarate to malate. Its importance extends beyond metabolism, as mutations in the FH gene can lead to various medical conditions, including fumarate hydratase deficiency and hereditary leiomyomatosis and renal cell cancer (HLRCC). Understanding FH's structure and function is essential for elucidating its role in these diseases and developing potential therapeutic strategies. Recombinant FH proteins have been produced to study enzyme kinetics, metabolic pathways, and the molecular basis of diseases linked to FH mutations. By characterizing the recombinant proteins, researchers aim to uncover insights into FH's enzymatic mechanisms and explore the impacts of different mutations. This information can aid in the design of targeted therapies and improve our understanding of the relationship between FH activity and cancer pathogenesis, highlighting the enzyme's significance in both metabolic processes and as a tumor suppressor.
