Recombinant Human Neuroserpin Protein Standard (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Neuroserpin also known by its alternate name Serpin I1 is a member of the serine protease inhibitor family. It weighs about 44 kDa. Neuroserpin expresses mainly in the nervous system particularly in the brain and spinal cord where it regulates proteolytic activity. It localizes to the endoplasmic reticulum and is secreted to the extracellular space influencing neural processes.

Biological function summary

Neuroserpin plays an important role in nervous system development and maintenance. It inhibits tissue plasminogen activator (tPA) a protease involved in breaking down blood clots and controls extracellular matrix modifications. Neuroserpin does not form part of a complex but interacts with other key proteins for its function. Its regulation of tPA influences synaptic plasticity and protection of neurons from excessive proteolysis which is essential in maintaining proper brain function.

Pathways

Neuroserpin's activity is significant in the plasminogen activation system and neurotrophic pathways. It influences the balance of proteolytic activities that affect cell migration and synaptic remodeling. Related proteins in these pathways include proteases like tPA and neurotrophins like brain-derived neurotrophic factor (BDNF) which support neuronal survival.

Mutations in neuroserpin are linked to familial encephalopathy with neuroserpin inclusion bodies (FENIB) and Alzheimer's disease. FENIB is caused by neuroserpin polymerization and accumulation leading to neurodegeneration. In Alzheimer's disease neuroserpin interaction with amyloid precursor protein pathways contributes to plaque formation and neuronal dysfunction. Neuroserpin's connection with defective tPA regulation underlies its association with these neurodegenerative conditions.