Analytical Data
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Gene name
NFU1
- Application
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Alternative Names
NFU1;HIRIP5;NFU1 iron-sulfur cluster scaffold homolog. 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
Q9UMS0
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Expression Region
10-254aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSGAAAVAAGLRRRFCHMLKNPYTIKKQP LHQFVQRPLFPLPAAFYHPVRYMFIQTQDTPNPNSLKFIPGKPVLETRTM DFPTPAAAFRSPLARQLFRIEGVKSVFFGPDFITVTKENEELDWNLLKPD IYATIMDFFASGLPLVTEETPSGEAGSEEDDEVVAMIKELLDTRIRPTVQ EDGGDVIYKGFEDGIVQLKLQGSCTSCPSSIITLKNGIQNMLQFYIPEVE GVEQVMDDESDEKEANSP
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Molecular Weight
30 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
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Protein Description
NFU1 (Nuclear-Factor Like 1) is a critical protein involved in the assembly of iron-sulfur (Fe-S) clusters, which are essential for many cellular processes, including electron transport, enzyme activity, and gene regulation. The proper functioning of NFU1 is crucial for maintaining cellular iron homeostasis and overall mitochondrial health. Mutations or dysfunctions in NFU1 have been linked to various diseases, including neurodegenerative disorders and mitochondrial dysfunctions. The study of NFU1 recombinant proteins is vital for understanding its structure-function relationship and the mechanisms by which it participates in Fe-S cluster biogenesis. Research has increasingly focused on the potential of NFU1 as a therapeutic target, given its role in iron metabolism and mitochondrial function. Additionally, recombinant NFU1 proteins can be utilized in biochemical assays to explore their interaction with other proteins, identify regulatory pathways, and investigate their potential in biotechnology applications. As such, the exploration of NFU1 through recombinant protein techniques not only advances our understanding of fundamental cellular processes but also holds promise for therapeutic interventions in diseases associated with iron-sulfur cluster biogenesis defects.
