Recombinant Human Neuroserpin protein (SERPINI1) (Active)
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Description
Functional Characteristics
Neuroserpin exerts its effects through protease inhibition and neuroprotective roles:
Key Functional Roles
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Protease Inhibition: Targets tissue-type plasminogen activator (tPA) and plasmin, regulating extracellular matrix (ECM) remodeling during synaptogenesis , , .
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Synaptic Plasticity: Facilitates synaptic connection formation and adaptation, critical for learning and memory , .
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Neuroprotection: Shields neurons from tPA-mediated excitotoxicity, particularly under pathological conditions , .
Mechanism of Action
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Utilizes a "suicide substrate" mechanism: Its reactive center loop (RCL) acts as bait for target proteases. Upon cleavage, conformational changes inactivate the protease irreversibly , .
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Structural stability is maintained by conserved β-sheets and α-helices, with dynamic regions like the RCL enabling inhibitory activity , .
Associated Diseases
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Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB): Caused by SERPINI1 mutations (e.g., His338Arg), leading to neuroserpin polymerization and neuronal degeneration , , .
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Epilepsy and Dementia: Linked to dysregulated synaptic plasticity and ECM degradation , .
Research Findings
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Structural Insights: Polymerization-prone mutants (e.g., Ser49Pro) destabilize β-sheet A, accelerating aggregation , .
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Therapeutic Potential: Recombinant neuroserpin reduces neuronal damage in models of stroke and glaucoma by inhibiting plasmin-mediated excitotoxicity .
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Disease Modeling: Transgenic mice lacking SERPINI1 exhibit motor neuron degeneration, mimicking FENIB pathology , .
Applications in Experimental Studies
Quality and Validation Standards
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Activity Validation: Confirmed via inhibition of tPA-mediated plasminogen activation , .
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Purity Assurance: Assessed by SDS-PAGE and mass spectrometry , .
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Batch Consistency: Rigorous quality control across ISO 9001-certified production facilities .
Limitations and Considerations
Product Specs
Buffer
Lyophilized from a 0.2 µm filtered PBS, pH 7.5
Form
Lyophilized powder
Lead Time
5-10 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% of glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers may use this as a reference.
Shelf Life
The shelf life is dependent on several factors, including storage state, buffer ingredients, storage temperature, and the stability of the protein itself.
Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.
Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquoting is necessary for multiple uses. Avoid repeated freeze-thaw
cycles.
Tag Info
Tag-Free
Synonyms
DKFZp781N13156; Neuroserpin; NEUS_HUMAN; Peptidase inhibitor 12; PI-12; PI12; Protease inhibitor 12 ; Serine or cysteine proteinase inhibitor clade I (neuroserpin) member 1; Serine or cysteine proteinase inhibitor clade I member 1; Serpin I1; Serpin peptidase inhibitor clade I (neuroserpin) member 1; SERPINI1
Datasheet & Coa
Please contact us to get it.
Expression Region
17-410aa
Mol. Weight
44.7 kDa
Protein Length
Full Length of Mature Protein
Purity
>95% as determined by SDS-PAGE.
Research Area
Neuroscience
Source
E.coli
Species
Homo sapiens (Human)
Target Names
SERPINI1
Uniprot No.
Target Background
Function
Neuroserpin is a serine protease inhibitor that selectively inhibits plasminogen activators and plasmin, but not thrombin. It may be involved in the formation or reorganization of synaptic connections, as well as in synaptic plasticity in the adult nervous system. Neuroserpin may protect neurons from cell damage caused by tissue-type plasminogen activator (tPA).
Gene References Into Functions
- Two pediatric cases of progressive myoclonic epilepsy with pathogenic variants in the SERPINI1 gene are presented, leading to a severe clinical presentation. PMID: 28631894
- Data suggests that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1, respectively, could be associated with a protective role in cerebral cavernous malformations disease. PMID: 27737651
- SERPINI1 plays a crucial role in regulating epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer. PMID: 26892864
- The thermal and chemical stability, along with the polymerization propensity of both Wild Type and Glu289Ala NS, were characterized. PMID: 26329378
- This C-terminal lability is not required for neuroserpin polymerization in the endoplasmic reticulum, but the additional glycan facilitates degradation of the mutant protein during proteasomal impairment. PMID: 26367528
- The protective effect of neuroserpin might be independent of its canonical interaction with tPA. PMID: 26176694
- Neuroserpin is expressed in naive effector memory and central memory CD4 and CD8 T cell subsets, as well as monocytes, B cells, and NK cells. T-cell activation causes its translocation to the immunologic synapse, secretion, and delayed downregulation. PMID: 25670787
- Molecular Dynamics simulations suggest that Neuroserpin conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds. PMID: 25450507
- Alzheimer's disease brain tissues with elevated neuroserpin protein also showed increased expression of THRbeta1 and HuD. PMID: 24036060
- This study did not provide any evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke. PMID: 21487809
- The origins of conformational lability were investigated. PMID: 21961602
- Neuroprotective properties of neuroserpin may be related to the inhibition of excitotoxicity, inflammation, as well as blood brain barrier disruption that occur after acute ischemic stroke. PMID: 21569344
- Hrd1 and gp78 mediate mutant neuroserpin turnover through the ERAD pathway. PMID: 21507957
- High serum neuroserpin levels before intravenous tPA and neuroserpin levels decrease at 24 h after ischemic stroke, independently of tPA treatment, may have a role in good functional outcome. PMID: 21174006
- The latent and polymer hNS forms obtained at 45 degrees C and 85 degrees C differ in their chemical and thermal stabilities; furthermore, the human neuroserpin polymers also differ in size and morphology. PMID: 21081089
- The refolding and polymerization pathways of wild-type neuroserpin and of the pathogenic mutants S49P and H338R were investigated. PMID: 20691191
- Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. PMID: 11880376
- The interactions between NSP and t-PA were distinct from those between plasmin and NSP, suggesting that the physiological effect of t-PA-NSP interactions may be more complex than previously thought. PMID: 12228252
- Neuroserpin has a role as a selective inhibitor of tPA in the central nervous system [review]. PMID: 14983220
- Neuroserpin mutants that cause dementia accumulate as polymers within the endoplasmic reticulum. PMID: 15090543
- tPA and neuroserpin are widely expressed in the human central nervous system. PMID: 15269833
- The reactive center loop of neuroserpin Portland is partially inserted into beta-sheet A to adopt a conformation similar to an intermediate on the polymerization pathway. PMID: 15291813
- Data show that the S49P mutant of neuroserpin that causes the dementia familial encephalopathy with neuroserpin inclusion bodies (FENIB) forms a latent species in vitro and in vivo in addition to the formation of polymers. PMID: 15664988
- Neuroserpin interacts with Abeta(1-42) to form off-pathway non-toxic oligomers and thus protects neurons in Alzheimer disease. PMID: 16849336
- The intergenic region of the head-to-head PDCD10-SERPINI1 gene pair provides an interesting and informative example of a complex regulatory system. PMID: 17212813
- In a French family with the S52R mutation of the neuroserpin gene, progressive myoclonic epilepsy was associated with a frontal syndrome. PMID: 17606885
- This study provides the first evidence that neuroserpin is associated with early-onset ischemic stroke among Caucasian women. PMID: 17961231
- Conformational modification in the protein under oxidative stress was observed. PMID: 18051703
- A neuroserpin mutation that causes electrical status epilepticus of slow-wave sleep is reported. PMID: 18591508
- Neuroserpin and tPA are associated with amyloid-beta plaques in Alzheimer brain tissue. PMID: 19222708
- Human neuroserpin: structure and time-dependent inhibition were investigated. PMID: 19265707
- Analyses restricted to glioblastoma (n = 254) yielded significant associations for the SELP, DEFB126/127, SERPINI1, and LY96 genetic regions. PMID: 19423540
- Intracellular neuroserpin polymers activate NF-kappaB by a pathway that is independent of the IRE1, ATF6, and PERK limbs of the canonical unfolded protein response but is dependent on intracellular calcium. PMID: 19423713
Database Links
Involvement In Disease
Encephalopathy, familial, with neuroserpin inclusion bodies (FENIB)
Protein Families
Serpin family
Subcellular Location
Secreted. Cytoplasmic vesicle, secretory vesicle lumen. Perikaryon.
Tissue Specificity
Detected in brain cortex and hippocampus pyramidal neurons (at protein level). Predominantly expressed in the brain.
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