Recombinant Human Neurofascin Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3479

Recombinant Human Neurofascin Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3479
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Product Overview

Tag Fc
Host Species Human
Accession NP_001005388.2
Synonym NF, NRCAML
Background NFASC, also known as neurofascin, belongs to the immunoglobulin superfamily, L1/neurofascin/NgCAM family. It contains 5 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains. NFASC functions in neurite outgrowth, neurite fasciculation, and organization of the axon initial segment (AIS) and nodes of Ranvier on axons during early development. Both the AIS and nodes of Ranvier contain high densities of voltage-gated Na+ (Nav) channels which are clustered by interactions with cytoskeletal and scaffolding proteins including this protein, gliomedin, ankyrin 3 (ankyrin-G), and betaIV spectrin. NFASC links the AIS extracellular matrix to the intracellular cytoskeleton.
Description A DNA sequence encoding the human NFASC (XP_011507630.1) (Met1-Gln939) was expressed with the Fc region of human IgG1 at the C-terminus.
Source HEK293
Predicted N Terminal Ile 25
AA Sequence Met1-Gln939
Molecular Weight The recombinant human NFASC consists 1156 a.a. and predicts a molecular mass of 130 kDa.
Purity >95% as determined by SDS-PAGE.
Endotoxin < 1.0 EU per μg protein as determined by the LAL method.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions.
Subcellular Location Cell membrane; Single-pass type I membrane protein.; [Isoform 8]: Cell junction, paranodal septate junction.
Protein Families Immunoglobulin superfamily, L1/neurofascin/NgCAM family
Database References

Gene Functions References

  1. data suggest that NFASC is a novel regulator of non-small cell lung cancer cell motility and support a role of NFASC in the regulation of non-small cell lung cancer progression PMID: 28418179
  2. identified neurofascin as the target of the autoantibodies in Chronic inflammatory demyelination polyneuropathy patients. PMID: 28575198
  3. #REF! PMID: 26843559
  4. It is a common protein to the central and peripheral nervous system may play a pivotal role in combined demyelination in Combined central and peripheral demyelination. PMID: 25672685
  5. Autoantibodies to NF155 identify a inflammatory demyelinating polyradiculoneuropathy subtype characterized by severe neuropathy, poor response to intravenous immunoglobulin, and disabling tremor. PMID: 24523485
  6. Anti-neurofascin antibody is frequently present in patients with CCPD. PMID: 23884033
  7. Three neuronal proteins (Huntingtin interacting protein 1, neurofascin, and olfactomedin-like 2a) are novel components of podocyte major processes and their expression in glomerular crescents supports their role in crescent formation. PMID: 22913984
  8. gliomedin, NF186, and contactin are novel target antigens in Guillain-Barre syndrome PMID: 22462667
  9. Neurofascin isoforms of 186, 180, 166 and 155 kDa are generated by alternative splicing and provide a switch between neuronal plasticity and stability. (Review) PMID: 22306302
  10. Cerebellar pinceau organization requires coordinated mechanisms involving specific neurofascin functions in both Purkinje and basket neurons. PMID: 22492029
  11. Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier PMID: 22009740
  12. two crystal structures of a dimeric form of the headpiece of neurofascin PMID: 21047790
  13. Nfasc isoforms use distinct protein-protein interaction modules to organize and stabilize specific axonal domains in myelinated axons. Loss of Nfasc immunoglobulin domains 5 and 6 in transgenic mice mimics complete ablation of Nfasc. PMID: 20371806
  14. in both mouse and human samples, the expression pattern of neurofascin 155(high) and neurofascin 155(low) is altered coincident with paranodal decay. PMID: 20129933
  15. different splicing variants of NF expressed on neurons and glia play distinct roles during neural development PMID: 16061393
  16. raft-association of NF155 is essential for the assembly of the paranodal junction and reduced association to lipid rafts is accompanied by the disassembly of the paranodal junction and contributes to the demyelination process in multiple sclerosis PMID: 17405145
  17. antibodies to neurofascin selectively targeted nodes of Ranvier, resulting in deposition of complement, axonal injury, and disease exacerbation PMID: 17846150
  18. a neurofascin intracellular domain activates FGFR1 for neurite outgrowth, whereas the extracellular domain functions as an additional, regulatory FGFR1 interaction domain in the course of development PMID: 19666467

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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