Recombinant Human Neurofascin (NFASC) Protein (His)

Name: Recombinant Human Neurofascin (NFASC) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10184P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Neurofascin (NFASC) Protein (His) is produced by our E.coli expression system. This is a cytoplasmic protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O94856
Target Symbol	NFASC
Synonyms	KIAA0756; Neurofascin; Neurofascin homolog; NF; Nfasc; NFASC_HUMAN; NRCAML
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KRSRGGKYPVREKKDVPLGPEDPKEEDGSFDYSDEDNKPLQGSQTSLDGTIKQQESDDSLVDYGEGGEGQFNEDGSFIGQYTVKKDKEETEGNESSEATSPVNAIYSLA
Expression Range	1239-1347aa
Protein Length	Cytoplasmic Domain
Mol. Weight	15.9kDa
Research Area	Cell Adhesion
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 29866 OMIM: 609145 KEGG: hsa:23114 STRING: 9606.ENSP00000344786 UniGene: PMID: 28418179 identified neurofascin as the target of the autoantibodies in Chronic inflammatory demyelination polyneuropathy patients. PMID: 28575198 #REF! PMID: 26843559 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 Autoantibodies to NF155 identify a inflammatory demyelinating polyradiculoneuropathy subtype characterized by severe neuropathy, poor response to intravenous immunoglobulin, and disabling tremor. PMID: 24523485 Anti-neurofascin antibody is frequently present in patients with CCPD. PMID: 23884033 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 gliomedin, NF186, and contactin are novel target antigens in Guillain-Barre syndrome PMID: 22462667 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 Cerebellar pinceau organization requires coordinated mechanisms involving specific neurofascin functions in both Purkinje and basket neurons. PMID: 22492029 Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier PMID: 22009740 two crystal structures of a dimeric form of the headpiece of neurofascin PMID: 21047790 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 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 different splicing variants of NF expressed on neurons and glia play distinct roles during neural development PMID: 16061393 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 antibodies to neurofascin selectively targeted nodes of Ranvier, resulting in deposition of complement, axonal injury, and disease exacerbation PMID: 17846150 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.