Cat: IPD-X32552

Recombinant Others nitA Protein

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Analytical Data

  • Gene name

    nitA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Aliphatic nitrilase

  • Species

    Others

  • Source

    E. coli

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q02068

  • Expression Region

    M1-K369

  • Protein Length

    Partial

  • 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

NitA is a recombinant protein that has garnered significant interest in the fields of microbiology and biotechnology due to its potential applications in various industrial processes and environmental remediation. NitA, commonly associated with nitrogen metabolism, is involved in the nitrogen cycle, where it plays a crucial role in the conversion of atmospheric nitrogen into forms usable by living organisms. The study of NitA includes understanding its structure, function, and the molecular mechanisms underlying its enzymatic activity. Additionally, research has focused on the optimization of its expression in host systems, which enables the large-scale production of this protein for further investigation. The ability to manipulate and utilize NitA opens avenues for biotechnological innovations, such as the development of biofertilizers, and enhances our understanding of nitrogen-fixing microorganisms. Moreover, as global issues related to nitrogen pollution and food security become increasingly pressing, the exploration of NitA and similar proteins is essential for developing sustainable agricultural practices and mitigating environmental impacts. This makes NitA not only a valuable subject of study in fundamental science but also a promising candidate for practical applications aimed at promoting ecological balance and agricultural efficiency.

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