Cat: IPD-X39291

Recombinant Rat NTE Protein,His

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Analytical Data

  • Gene name

    NTE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PNPLA6; Sws; Patatin-Like Phospholipase Domain Containing 6

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    M0R715

  • Expression Region

    Leu965~Thr1137

  • Molecular Weight

    23kDa

  • 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

NTE (Neuropathy Target Esterase) is a crucial enzyme involved in lipid metabolism and has garnered significant attention in the field of neurobiology due to its association with various neurodegenerative diseases. Mutations in the NTE gene have been implicated in conditions like the hereditary sensory and autonomic neuropathy type II. Historically, NTE has been recognized for its role in the hydrolysis of phospholipids, thus playing a vital part in cellular signaling and membrane integrity. Research into the recombinant expression of NTE has expanded our understanding of its structure and function, allowing for the investigation of its enzymatic activity and interactions with other cellular components. Recombinant NTE proteins are valuable for studying the biochemical pathways in which NTE is involved, as well as elucidating the mechanisms by which mutations can lead to disease. Furthermore, the ability to produce NTE in a controlled laboratory setting opens avenues for developing therapeutic strategies aimed at mitigating the effects of NTE-related pathologies. The advancements in recombinant DNA technology have also facilitated more detailed studies of NTE's functional domains and regulatory mechanisms, enhancing our understanding of its multifaceted roles in health and disease. Overall, NTE's significant implications in neuroscience and its potential as a therapeutic target underscore the importance of ongoing research in this area.

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