Cat: IPD-X27970

Recombinant Human Neurofascin Protein (HEK293),hFc

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Analytical Data

  • Gene name

    Neurofascin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Neurofascin; NFASC; KIAA0756

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-hFc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O94856-12

  • Expression Region

    I25-Q939

  • Protein Length

    Partial

  • 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

Neurofascin is a member of the immunoglobulin superfamily and is predominantly expressed in the nervous system, playing a crucial role in the development and maintenance of the myelin sheath in peripheral and central nervous systems. It functions as a cell adhesion molecule, facilitating the interactions between neurons and glial cells. The study of recombinant neurofascin proteins has gained considerable attention due to their potential implications in understanding neurodevelopmental disorders and demyelinating diseases such as multiple sclerosis. By examining the structure-function relationship of neurofascin, researchers aim to elucidate the molecular mechanisms underlying neural connectivity and myelin stability. Furthermore, recombinant neurofascin can be utilized in therapeutic applications, including the development of strategies for enhancing nerve regeneration and repair after injury. The expression of neurofascin in various isoforms, particularly neurofascin-186 and neurofascin-155, highlights the complexity of its functions and regulatory mechanisms. Investigations into the signaling pathways activated by neurofascin interaction with its ligands are critical for deciphering its role in neuronal plasticity and signaling transduction in health and disease. Overall, the exploration of neurofascin recombinant proteins represents a promising frontier in neuroscience research, with the potential to provide insights into fundamental biological processes and novel therapeutic targets in neuropathological conditions.

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