Analytical Data
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Gene name
nifH
- Application
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Alternative Names
Nitrogenase Fe protein Nitrogenase component II Nitrogenase reductase
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Species
Rhizobium leguminosarum
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Source
E. coli
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Tag
N- His-GST & C- Myc
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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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Molecular Weight
35 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 for the nitrogenase enzyme's Fe protein, which plays a critical role in biological nitrogen fixation, a process whereby atmospheric nitrogen (N2) is converted into ammonia (NH3), a form usable by plants. Understanding the function and structure of NifH is essential for biotechnology applications, particularly in enhancing nitrogen fixation in crops to reduce reliance on synthetic fertilizers. The study of recombinant NifH proteins allows researchers to investigate the enzyme's catalytic mechanisms, interactions with other nitrogenase components, and its regulation under different environmental conditions. Moreover, advancements in recombinant DNA technology have facilitated the production of NifH proteins in various expression systems, making it possible to analyze their biochemical properties in detail. Research focusing on the recombinant form of NifH not only contributes to the fundamental understanding of nitrogenase functionality but also paves the way for genetic engineering approaches in agricultural practices aimed at improving nitrogen use efficiency and sustainable crop production. The integration of knowledge from structural biology, molecular biology, and bioinformatics in NifH research underscores its importance in addressing global challenges related to food security and environmental sustainability.
