Cat: IPD-X24342

Recombinant Human NEFL Protein,His & SUMO

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Analytical Data

  • Gene name

    NEFL

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (NF-L)(68 kDa neurofilament protein)(Neurofilament triplet L protein)

  • Species

    Human

  • Source

    E. coli

  • Tag

    C- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P07196

  • Expression Region

    50-400aa

  • Molecular Weight

    52.4 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

NEFL (Neurofilament Light Chain) is a critical protein component of the neurofilament cytoskeleton in neurons, playing a vital role in maintaining the structural integrity and function of neurons. Research into NEFL has gained momentum due to its association with various neurological disorders, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and other neurodegenerative conditions. The abnormal accumulation or altered expression of NEFL has been observed in these pathologies, indicating its potential as a biomarker for disease progression and diagnosis. Additionally, NEFL has garnered interest in the context of neural regeneration and the response of neurons to injury. Recent advancements in recombinant protein technology have facilitated the production of NEFL for in-depth studies, enabling researchers to investigate its biochemical properties, structure-function relationships, and interactions with other cellular components. The use of recombinant NEFL is instrumental in elucidating its role in neurobiology and the cellular mechanisms underlying neurodegeneration and repair. As such, NEFL's importance extends beyond being a mere structural protein; it serves as a pivotal target for therapeutic interventions and a tool for understanding the intricate dynamics of neuronal health and disease.

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