Cat: IPD-X28633

Recombinant Human NaCT Protein (Baculovirus)

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Analytical Data

  • Gene name

    NaCT

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NACT

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86YT5-1

  • Expression Region

    M1-T568

  • Protein Length

    Full Length of Isoform-1

  • 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.

Quality inspection process

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Protein Description

NaCT (N-acetyltransferase) is a key enzyme involved in the metabolism of various substances, including drugs and endogenous compounds. Its primary function is to catalyze the transfer of an acetyl group from acetyl-CoA to various amines, which can influence the pharmacokinetics and toxicity of many pharmacological agents. The study of NaCT has gained significant attention due to its implications in drug metabolism, therapeutic efficacy, and individual variability in drug response. Recent advances in recombinant protein technology have enabled researchers to produce purified NaCT for in vitro studies, facilitating the elucidation of its structure, function, and interactions with other biomolecules. Understanding NaCT's role may provide insights into its potential as a therapeutic target and its involvement in diseases linked to altered drug metabolism, such as cancer and metabolic disorders. Additionally, the development of specific inhibitors or activators of NaCT could enhance drug safety profiles and personalized medicine approaches. The ongoing research on NaCT aims to uncover its detailed mechanisms and explore its relevance in both basic and clinical pharmacology.

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