Analytical Data
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Gene name
FUM
- Application
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Alternative Names
FUM；SDH2；SDHF；Succinate dehydrogenase [ubiquinone] flavoProtein subunit. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P93033
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Expression Region
1-492aa
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AA Sequence
MSIYVASRRLSGGTTVTALRYATSLRSYSTSFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGVLKKCAAKVNMEYGLDPTIGKAIMQAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGRKRGEKCVHPNDHVNRSQSSNDTFPTVMHIAAATEINSRLIPSLKTLHSTLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVKYGLNRVTCTLPRLYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELVLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTVGGSNGHFELNVFKPVIASALLHSVRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKKAHKEGCTLKEAALNLGVLTAEEFDTLVVPEKMIGPSD
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Molecular Weight
53 kDa
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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
FUM recombinant protein, derived from the fungus Fusarium, has garnered significant attention in the field of biotechnology and molecular biology due to its potential applications in agriculture, food safety, and pharmaceuticals. The increasing prevalence of fungal pathogens in crops necessitates the exploration of effective biological control agents, and FUM protein has shown promise in enhancing plant resistance to various diseases. Additionally, its role in the production of mycotoxins, toxic compounds often found in contaminated food products, highlights the need for a deeper understanding of its mechanisms. Researchers are actively investigating the molecular structure and function of FUM recombinant protein, aiming to elucidate its interactions with plant systems and the microbiome. This research may lead to innovative strategies for developing transgenic crops with improved resilience against fungal infections and reduced mycotoxin contamination. Furthermore, the ability to produce FUM protein through recombinant DNA technology allows for more scalable and sustainable approaches to mitigate the economic impact of agricultural losses caused by fungi. In summary, the study of FUM recombinant protein is pivotal not only for enhancing agricultural sustainability and food safety but also for contributing to the broader understanding of plant-fungal interactions and mycotoxin management.
