Analytical Data
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Gene name
FE
- Application
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Alternative Names
FE；Cytosolic Fe-S cluster assembly factor NUBP2
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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
Q9Y5Y2
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Expression Region
1-271aa
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AA Sequence
MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP
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Molecular Weight
28.8 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
The study of FE (ferrous iron) recombinant proteins has emerged as a significant area of research due to their critical roles in various biological processes, including cellular metabolism, oxygen transport, and electron transfer. Iron is an essential element for nearly all living organisms, and its proper regulation is vital for maintaining cellular functions and overall health. Recombinant protein technology allows scientists to produce large quantities of these proteins in a controlled environment, facilitating in-depth studies of their structure, function, and mechanisms. Recent advancements in molecular biology techniques have enabled researchers to manipulate genes encoding FE proteins, enhancing our understanding of their roles in iron homeostasis and related disorders such as anemia and hemochromatosis. Furthermore, the engineering of FE proteins holds potential applications in biotechnology and pharmaceuticals, such as in the development of targeted therapies or novel biomaterials. As the understanding of iron metabolism continues to evolve, the exploration of FE recombinant proteins promises to unveil new insights into both fundamental biology and practical applications in health and disease management.
