Analytical Data
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Gene name
nfuA
- Application
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Alternative Names
nfuA；gntY；yhgI；Fe/S biogenesis Protein NfuA
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Species
E.coli
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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
B1X760
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Expression Region
1-191aa
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AA Sequence
MIRISDAAQAHFAKLLANQEEGTQIRVFVINPGTPNAECGVSYCPPDAVEATDTALKFDLLTAYVDELSAPYLEDAEIDFVTDQLGSQLTLKAPNAKMRKVADDAPLMERVEYMLQSQINPQLAGHGGRVSLMEITEDGYAILQFGGGCNGCSMVDVTLKEGIEKQLLNEFPELKGVRDLTEHQRGEHSYY
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Molecular Weight
68.8 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
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Protein Description
The nfuA gene, which encodes a protein involved in the iron-sulfur cluster assembly, has garnered significant attention in the field of molecular biology due to its vital role in cellular metabolism and stress responses. Iron-sulfur clusters are essential cofactors for a variety of enzymes, playing crucial roles in electron transport, respiration, and photosynthesis. In microorganisms, nfuA is particularly important for the management of iron and sulfur, which are key elements for growth and survival. Disruption of nfuA function has been linked to decreased cellular viability and impaired metabolic processes, highlighting its importance in maintaining iron homeostasis. Research on recombinant nfuA protein aims to elucidate its structure, function, and mechanisms of action, which can provide insights into larger biological systems and potential applications in biotechnology. Understanding the properties of nfuA can lead to advancements in developing new strategies for managing iron-related diseases and enhancing microbial processes utilized in bioremediation and bioenergy production. Investigating the recombinant expression of nfuA also presents opportunities for exploring its interactions with other cellular components, offering a deeper understanding of the complex interplay between iron-sulfur cluster assembly and cellular physiology. Overall, nfuA represents a promising target for further research, with implications ranging from basic biochemistry to practical applications in health and environmental sustainability.
