Analytical Data
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Gene name
fum
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简介
Fum proteins crucially catalyze the interconversion of fumarate to L-malate in the tricarboxylic acid (TCA) cycle, maintaining metabolite flow in cellular energy metabolism. This critical step, if precisely regulated, helps generate energy and generates intermediates critical to cellular processes. fum Protein, Corynebacterium glutamicum (His) is the recombinant fum protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
fumC; Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase
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Species
Others
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NRN8
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Expression Region
M1-F469
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Protein Length
Partial
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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
FUM recombinant protein research focuses on the study and application of fumarate hydratase (FUM), an enzyme involved in the citric acid cycle, which plays a crucial role in cellular metabolism. This enzyme catalyzes the reversible hydration of fumarate to malate, and its dysfunction is associated with various metabolic disorders and certain cancers, particularly hereditary leiomyomatosis and renal cell cancer (HLRCC). Scientists are increasingly interested in FUM for its potential therapeutic applications, as understanding its structure and function can lead to novel treatments for such diseases. Advancements in genetic engineering and recombinant DNA technology have enabled the efficient production of FUM, allowing researchers to explore its enzymatic properties, optimize its activity for industrial applications, and develop inhibitors or activators for therapeutic interventions. Moreover, elucidating the molecular mechanisms underlying FUM function and its role in metabolic pathways can provide insights into tumorigenesis and metabolic regulation, promoting the development of targeted therapies. The growing body of literature on FUM underscores its significance in biochemistry and medicine, highlighting the potential for recombinant FUM in therapeutic applications and its importance in understanding complex metabolic processes.
