Analytical Data
-
Gene name
Neurofascin
- Application
-
Alternative Names
Neurofascin; NFASC; KIAA0756
-
Species
Human
-
Source
HEK293
-
Tag
C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O94856-12
-
Expression Region
I25-Q939
-
Protein Length
Partial
-
Molecular Weight
114-119 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
-
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
Related Products
Protein Description
Neurofascin is a member of the immunoglobulin superfamily and is primarily expressed in the nervous system, playing critical roles in neuronal development and myelination. It exists in two primary isoforms—Neurofascin 155 and Neurofascin 186—which are localized at different sites in the neuron: Neurofascin 155 is found in the nodes of Ranvier and is crucial for the proper conduction of action potentials, while Neurofascin 186 is associated with myelinating glial cells and is involved in the formation of axoglial junctions. Given its importance in neural function and the pathophysiology of neurodegenerative diseases, including Multiple Sclerosis and Charcot-Marie-Tooth disease, research on Neurofascin recombinant proteins has gained significance. These recombinant proteins are utilized to study their structural properties, binding interactions, and functional roles in cell adhesion and signaling pathways. The study of Neurofascin not only enhances our understanding of neuronal communication and myelination but also opens avenues for potential therapeutic strategies targeting demyelinating diseases. As such, the development and characterization of Neurofascin recombinant proteins are pivotal for both basic neuroscience research and clinical applications.
