SERPINI1 Human, His
Description
Compound Identification and Structure
SERPINI1 Human, His is a recombinant form of the SERPINI1 protein (UniProt: Q99574), which belongs to the serpin superfamily. Key features include:
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Amino Acid Sequence: Comprises 404 residues (aa 17–410) with a 10-amino acid N-terminal His tag .
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Post-Translational Modifications: Non-glycosylated due to prokaryotic expression .
The protein adopts the conserved serpin fold, featuring a reactive center loop (RCL) critical for protease inhibition . Structural dynamics, including RCL flexibility, influence its inhibitory activity and polymerization propensity .
Expression and Purification
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Purification: Proprietary chromatographic techniques yield >95% purity (SDS-PAGE) .
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Formulation: Lyophilized powder in phosphate buffer (pH 7.4) .
Physical Properties
| Property | Specification | Source |
|---|---|---|
| Solubility | ≥100 µg/ml in sterile H₂O | |
| Stability | -20°C (lyophilized); 4°C (reconstituted) | |
| Reconstitution | 0.5 mg/ml in deionized water |
Biological Functionality
SERPINI1 inhibits tissue-type plasminogen activator (tPA) and plasmin, modulating extracellular matrix (ECM) remodeling during synaptogenesis . Key roles include:
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Neuroprotection: Prevents axonal degradation in murine models .
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Synaptic Plasticity: Regulates ECM proteolysis to facilitate neuronal adaptation .
Activity Assay
Neurodegenerative Disease Models
Mutations in SERPINI1 (e.g., Ser49Pro, Gly392Arg) cause familial encephalopathy with neuroserpin inclusion bodies (FENIB), characterized by neuronal polymer accumulation . Recombinant SERPINI1 aids in studying these mechanisms.
Therapeutic Potential
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Glaucoma Neuroprotection: Intravitreal administration in murine glaucoma models preserved retinal ganglion cell density and electrophysiological function (pSTR amplitude: p < 0.01 vs. untreated controls) .
Clinical and Industrial Relevance
Product Specs
Product Science Overview
Serpin Peptidase Inhibitor, Clade I Member 1, also known as Neuroserpin, is a member of the serpin superfamily of serine proteinase inhibitors. This protein is encoded by the SERPINI1 gene and is primarily secreted by axons in the brain . The recombinant form of this protein, tagged with a His (histidine) tag, is often used in research to facilitate purification and detection.
The primary function of Neuroserpin is to regulate the activity of tPA, which is involved in the breakdown of blood clots. By inhibiting tPA, Neuroserpin helps to protect neurons from damage and supports the formation and reorganization of synaptic connections . This function is essential for maintaining synaptic plasticity in the adult nervous system.
The activity of Neuroserpin is regulated at multiple levels, including gene expression, post-translational modifications, and interactions with other proteins. Mutations in the SERPINI1 gene can lead to the accumulation of mutant Neuroserpin polymers, resulting in a condition known as familial encephalopathy with Neuroserpin inclusion bodies (FENIB) . This condition is characterized by the progressive accumulation of Neuroserpin aggregates in the brain, leading to neurodegeneration and epilepsy.
The recombinant form of Neuroserpin, tagged with a His tag, is widely used in research to study its structure, function, and interactions with other proteins. The His tag allows for easy purification and detection of the protein, facilitating various biochemical and biophysical analyses.
