Cat: IPD-X40782

Recombinant Candida albicans FBA1 Protein ,His & Myc

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Analytical Data

  • Gene name

    FBA1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    37 kDa major allergen (Fructose-1,6-bisphosphate aldolase) (IgE-binding allergen) (FBP aldolase) (FBPA)

  • Species

    Candida albicans

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9URB4

  • Expression Region

    2-359aa

  • Molecular Weight

    46.5 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

FBA1, or fructose-bisphosphate aldolase 1, is an enzyme that plays a crucial role in the glycolytic pathway, catalyzing the reversible conversion of fructose-1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde-3-phosphate. Research on FBA1 has garnered interest due to its significance in cellular metabolism, energy production, and its potential implications in various diseases, including cancer and metabolic disorders. The study of FBA1 recombinant protein allows for a better understanding of its structural and functional properties, enabling researchers to investigate its enzymatic mechanism, regulation, and interactions with other metabolic pathways. Furthermore, characterizing FBA1 as a recombinant protein facilitates its use in biochemical assays and drug development, providing insights into the design of inhibitors or modulators that could have therapeutic applications. By elucidating the role of FBA1 in cellular processes and its involvement in pathophysiological conditions, scientists aim to uncover new targets for therapeutic intervention and develop strategies to modulate its activity for clinical benefits. Overall, the investigation of FBA1 recombinant protein lies at the intersection of biochemistry, molecular biology, and pharmacology, holding promise for advancing our understanding of metabolic diseases and developing targeted treatment strategies.

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