Analytical Data
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Gene name
NFASC
- Application
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Alternative Names
NFASC；KIAA0756；Neurofascin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O94856
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Expression Region
1239-1347aa
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AA Sequence
KRSRGGKYPVREKKDVPLGPEDPKEEDGSFDYSDEDNKPLQGSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
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Molecular Weight
15.9kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
NFASC (Neurofascin) is a member of the fasciclin family of cell adhesion molecules, predominantly expressed in the nervous system. It plays a crucial role in axonal ensheathment by glial cells and is vital for the formation and maintenance of the nodes of Ranvier, which are essential for rapid nerve conduction. Research into NFASC has gained momentum due to its association with various neurological disorders, including multiple sclerosis and schizophrenia, where its disruption may contribute to myelin sheath pathology and impaired neuronal signaling. Understanding the structure and function of NFASC through recombinant protein studies can provide insights into its adhesive properties and interactions with other cellular components. This knowledge is important not only for elucidating the mechanisms underlying nerve function but also for potential therapeutic interventions aimed at repairing myelin and restoring neurological function. Techniques such as expression in heterologous systems, purification, and characterization of recombinant NFASC proteins are instrumental in advancing our comprehension of its biological roles and the molecular pathways it influences in both health and disease. Furthermore, the development of NFASC-targeted therapies could pave the way for novel treatment modalities for demyelinating diseases and other CNS disorders. With the growing interest in neurobiology and regenerative medicine, NFASC serves as a significant focus for ongoing research aimed at enhancing our understanding of myelination and nerve repair.
