NRN1 Human

Neuritin-1 Human Recombinant
Cat. No.
BT10499
Source
Escherichia Coli.
Synonyms
Neuritin 1, NRN1, NRN, dJ380B8.2, Neuritin.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Human NRN1 produced in E.coli cells is a non-glycosylated, homodimeric protein containing 2x88 amino acid chains and having a molecular mass of 19.4kDa.
The NRN1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neuritin (NRN1) is a neurotrophic factor that plays a crucial role in the development and function of the nervous system. Its expression is induced by neuronal activity and growth factors such as NGF, BDNF, and NT3. NRN1 is primarily found in differentiating neurons during development and in areas associated with synaptic plasticity in the adult brain. It contributes to neurite outgrowth, neuronal survival, and the maturation of synapses.
Description
Recombinant Human NRN1, produced in E.coli cells, is a non-glycosylated protein composed of two identical chains, each containing 88 amino acids. This homodimeric structure results in a molecular weight of 19.4kDa. The purification process involves specialized chromatographic techniques to ensure high purity.
Physical Appearance
White powder, sterile, and freeze-dried.
Formulation
The NRN1 has been freeze-dried from a solution containing 0.2 µm filtered 1X PBS with a pH of 7.4.
Solubility
To reconstitute the freeze-dried NRN1, it is recommended to dissolve it in sterile 18M-cm H₂O at a concentration of at least 100 µg/ml. This solution can be further diluted with other aqueous solutions as needed.
Stability
Lyophilized NRN1 remains stable for 3 weeks at room temperature but should be stored in dry conditions below -18°C. After reconstitution, store NRN1 at 4°C for a maximum of 2-7 days. For long-term storage, freeze NRN1 below -18°C. It is advisable to add a carrier protein (0.1% HSA or BSA) for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using the following methods: (a) Analysis by RP-HPLC (Reverse Phase High-Performance Liquid Chromatography), and (b) Analysis by SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis).
Biological Activity
The ED₅₀, determined through a cell proliferation assay using rat C6 cells, is less than 25 ng/ml. This corresponds to a specific activity of greater than 4.0 x 10⁴ IU/mg.
Synonyms
Neuritin 1, NRN1, NRN, dJ380B8.2, Neuritin.
Source
Escherichia Coli.
Amino Acid Sequence
AGKCDAVFKG FSDCLLKLGD SMANYPQGLD DKTNIKTVCT YWEDFHSCTV TALTDCQEGA KDMWDKLRKE SKNLNIQGSL FELCGSGN.

Product Science Overview

Gene and Protein Structure

The NRN1 gene is located on chromosome 6 and encodes a protein that is expressed in postmitotic-differentiating neurons. This protein is particularly associated with neuronal structures involved in plasticity in the adult nervous system . The expression of NRN1 can be induced by neural activity and neurotrophins, which are proteins that promote the survival, development, and function of neurons .

The Neuritin-1 protein contains a consensus cleavage signal found in glycosylphosphatidylinositol (GPI)-anchored proteins. This signal is essential for the protein’s attachment to the cell membrane, which is crucial for its function in promoting neurite outgrowth and arborization .

Function and Mechanism

Neuritin-1 is known to promote neurite outgrowth and branching of neuritic processes, particularly in primary hippocampal and cortical cells . This function is vital for the formation and maintenance of neural networks, which are essential for learning, memory, and overall brain function.

The protein’s role in promoting neuritogenesis (the process of forming new neurites) suggests its importance in neural development and repair. Studies have shown that Neuritin-1 is upregulated in injured nerves, indicating its involvement in nerve repair and regeneration .

Recombinant Neuritin-1

Recombinant Neuritin-1 is produced using an E. coli expression system. The recombinant protein is typically purified to a high degree of purity and is used in various research applications to study its function and potential therapeutic uses . The recombinant form of Neuritin-1 retains the biological activity of the native protein, making it a valuable tool for studying neural development and plasticity.

Clinical and Research Implications

Overexpression of Neuritin-1 has been associated with the progression of astrocytoma, a type of brain tumor . This suggests that while Neuritin-1 plays a beneficial role in neural development and repair, its dysregulation can contribute to pathological conditions.

Research into Neuritin-1 continues to explore its potential therapeutic applications, particularly in the context of neurodegenerative diseases and nerve injury. By understanding the mechanisms through which Neuritin-1 promotes neurite outgrowth and neural plasticity, scientists hope to develop new treatments for conditions that affect the nervous system.

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