Analytical Data
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Gene name
nifH
- Application
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Alternative Names
nifH；Nitrogenase iron Protein
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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
P20623
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Expression Region
1-47aa
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AA Sequence
MAALRQIAFYGKGGIGKSTTSQNTLAALVDHHVPRIPMIIRIGGYAQ
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Molecular Weight
35.0 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 nifH gene encodes a critical component of the nitrogenase enzyme complex responsible for nitrogen fixation in various bacteria, including those forming symbiotic relationships with plants. Research on recombinant NifH proteins has gained attention due to their potential applications in agriculture and biotechnology, particularly in improving soil fertility and crop productivity by enhancing nitrogen availability. Understanding the structure and function of NifH at the molecular level is vital, as this enables scientists to elucidate the enzymatic mechanisms involved in nitrogen fixation. Moreover, advances in genetic engineering and protein expression technologies have facilitated the production of recombinant NifH proteins, allowing researchers to study their activity, stability, and interaction with other nitrogenase components. Investigating these proteins can provide insights into the evolutionary adaptations of nitrogen-fixing organisms and may lead to innovative strategies for developing biofertilizers or engineering nitrogen-fixing capabilities in non-leguminous crops, thereby promoting sustainable agricultural practices. This research not only addresses the pressing need for sustainable food production in the face of global challenges such as climate change and soil depletion but also contributes to a fundamental understanding of nitrogen metabolism in the biosphere.
