Cat: IPD-X40236

Recombinant Methanobacterium ivanovii nifH1 Protein ,His & Myc

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Analytical Data

  • Gene name

    nifH1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Nitrogenase Fe protein 1 (Nitrogenase component II) (Nitrogenase reductase)

  • Species

    Methanobacterium ivanovii

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P51602

  • Expression Region

    1-275aa

  • Molecular Weight

    37.4 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

The nifH gene encodes a nitrogenase enzyme component essential for nitrogen fixation, a critical biological process enabling the conversion of atmospheric nitrogen into a form that can be utilized by living organisms. Research into the nifH1 recombinant protein has gained prominence due to its potential applications in agriculture and biotechnology, particularly in enhancing soil fertility and crop productivity through biological nitrogen fixation. Given the global challenge of food security and the environmental impacts of synthetic fertilizers, understanding the structure and function of nifH1 can provide insights into developing sustainable agricultural practices. Advances in molecular biology techniques, such as recombinant DNA technology, have facilitated the production of nifH1 proteins in model organisms, allowing for detailed studies of their biochemical properties and interactions. These studies aim to elucidate the mechanisms underlying nitrogen fixation and explore ways to optimize these pathways for practical applications. Additionally, nifH1 serves as a valuable marker in environmental microbiology for assessing the presence and activity of nitrogen-fixing bacteria in different ecosystems, thus contributing to our understanding of global nitrogen cycles and ecosystem health. Overall, the study of nifH1 recombinant protein is pivotal in addressing ecological and agricultural challenges while promoting sustainable practices in nitrogen management.

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