Cat: IPD-X40408

Recombinant Neurospora crassa aro-2 Protein ,His

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Analytical Data

  • Gene name

    aro-2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    5-enolpyruvylshikimate-3-phosphate phospholyase

  • Species

    Neurospora crassa

  • Source

    E. coli

  • Tag

    C- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q12640

  • Expression Region

    1-432aa

  • Molecular Weight

    46.8 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 Aro-2 recombinant protein, derived from the Aro-2 gene, plays a significant role in the metabolic pathways of microorganisms, particularly in the biosynthesis of aromatic amino acids. Research into Aro-2 has gained momentum due to its potential applications in biotechnology and pharmaceuticals. Aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan, are essential for protein synthesis and serve as precursors for numerous bioactive compounds. The manipulation of Aro-2 expression and activity can lead to enhanced production of these amino acids in microbial strains, improving yields in industrial fermentation processes. Furthermore, studying Aro-2 provides insights into the regulation of metabolic pathways, allowing researchers to explore engineered strains with optimized amino acid profiles for diverse applications, ranging from food additives to therapeutic agents. Investigations into the structural and functional characteristics of the Aro-2 protein can facilitate the development of innovative biotechnological strategies, addressing challenges in sustainable production and resource utilization. Overall, Aro-2 represents a promising focus for ongoing research aimed at harnessing microbial metabolism for beneficial purposes.

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