NRN1 Human, His

Neuritin-1 expression is induced by neural activity and neurotrophins such as nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and neurotrophin-3 (NT3) . The protein promotes neurite outgrowth and branching of neuritic processes, which are essential for the formation and maintenance of neural networks . Additionally, Neuritin-1 supports neuronal survival and synaptic maturation, making it a key player in neurodevelopment and synaptic plasticity .

Human Recombinant Neuritin-1 (His Tag) is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain consisting of 99 amino acids, including a 10 amino acid His tag at the N-terminus . The His tag facilitates purification and detection of the recombinant protein. The total calculated molecular mass of the recombinant protein is approximately 11.02 kDa .

The recombinant protein is typically provided as a lyophilized (freeze-dried) powder and can be reconstituted in deionized water to prepare a working stock solution . It is important to filter the reconstituted protein using an appropriate sterile filter before using it in cell culture to ensure sterility .

Recombinant Neuritin-1 is used in various laboratory research applications, including studies on neurite outgrowth, neuronal survival, and synaptic plasticity. It is also utilized in experiments investigating the molecular mechanisms underlying neurodevelopmental processes and neurodegenerative diseases .

The lyophilized recombinant Neuritin-1 protein should be stored at -20°C to maintain its stability . After reconstitution, the protein should be aliquoted to avoid repeated freeze-thaw cycles, which can degrade the protein. Reconstituted protein can be stored at 4°C for a limited period .

Neuritin-1 (Human Recombinant, His Tag) is intended for laboratory research use only and should not be used as drugs, agricultural or pesticidal products, food additives, or household chemicals .