Recombinant Human Neuritin Protein (N-6His)

Name: Recombinant Human Neuritin Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-0882NP
Availability: InStock

BL-0882NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality cytokines for advanced research, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Neuritin is produced by our E.coli expression system and the target gene encoding Ala28-Gly116 is expressed with a 6His tag at the N-terminus.
Accession	Q9NPD7
Synonym	Neuritin;NRN1;NRN
Gene Background	Neuritin/NRN1 is a member of the neuritin family and can be expressed in postmitotic-differentiating neurons of the developmental nervous system and neuronal structures associated with plasticity in the adult. Neuritin/NRN1 promotes neurite outgrowt， arborization and neuritogenesis. The protein contains a consensus cleavage signal found in glycosylphoshatidylinositol (GPI)-anchored proteins.Overexpression of the encoded protein may be associated with astrocytoma progression.
Molecular Mass	12.1 KDa
Apmol Mass	10 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor. Cell junction, synapse.
Protein Families	Neuritin family
Database References	HGNC: 17972 OMIM: 607409 KEGG: hsa:51299 STRING: 9606.ENSP00000244766 UniGene: PMID: 27901477 results suggest that DTNBP1 and NRN1 genes show a joint effect on the risk for schizophrenia spectrum disorders. Although the precise mechanism underlying this effect is unclear, the fact that these genes have been involved in synaptic maturation, connectivity and glutamate signalling suggests that our findings could be of value as a link to the schizophrenia aetiology. PMID: 27855309 NRN1 is associated with depressive symptoms and executive function in a non-clinical sample. Our results also suggest that the role of NRN1 seems to be modulated by BDNF. PMID: 28107668 On analysis of the expression of NRN1 in SMA patients for the first time, NRN1 could be a potential modifier gene PMID: 27279027 Ca(2+)/calcineurin (CaN)/nuclear factor of activated T-cells (NFAT) c4 axis is required for neuritin-induced Kv4.2 transcriptional expression and potentiation of IA densities in cerebellum granule neurons. PMID: 27307045 (i) NRN1 variability is a shared risk factor for both schizophrenia-spectrum disorders (SSD) and bipolar disorders (BPD), (ii) NRN1 may have a selective impact on age at onset and intelligence in SSD. PMID: 26700405 Data indicate that neuritin not only plays an important role in the nervous system but also has an effect on the migration, senescence, proliferation, and viability of stem cells PMID: 26208391 Neuritin is reduced in the brains of Alzheimer's disease (AD) patients. PMID: 25101829 MiR-204 promotes apoptosis in oxidative stress-induced rat Schwann cells by suppressing neuritin expression PMID: 25036738 we found neuritin is overexpressed in astrocytoma, which may be an important factor in tumorigenesis and progression of astrocytoma PMID: 20405246 Data show that SMN and HuD form a complex in spinal motor axons, and that both interact with cpg15 mRNA in neurons. PMID: 21652774 NRN1 polymorphisms have roles in fluid intelligence in schizophrenia PMID: 19569075 CPG15 and CPG15-2 perform similar cellular functions but may play distinct roles in vivo through their cell-type- and tissue-specific transcriptional regulation PMID: 18265009

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.