Product Details

Purity

>95% as determined by SDS-PAGE.

Endotoxin

Less than 1.0 EU/μg as determined by LAL method.

Activity

Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 0.5 μg/ml, corresponding to a specific activity of >2000 IU/mg.

Target Names

SERPINI1

Uniprot No.

Q99574

Research Area

Neuroscience

Alternative Names

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

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

17-410aa

Complete Sequence

TGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQGSTQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDLVSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLATLEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL

Mol. Weight

44.7 kDa

Protein Length

Full Length of Mature Protein

Tag Info

Tag-Free

Form

Lyophilized powder

Buffer

Lyophilized from a 0.2 µm filtered PBS, pH 7.5

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 to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

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.

Datasheet & COA

Please contact us to get it.

Description

Neuroserpin (SERPINI1) is a critical serine protease inhibitor in the CNS that regulates tissue-type plasminogen activator activity, making its functional characterization essential for understanding neuroprotective mechanisms and neurodegenerative pathology. This tag-free recombinant human neuroserpin, spanning residues 17–410 of the mature protein, demonstrates an ED50 of less than 0.5 μg/ml in a rat C6 cell proliferation assay, corresponding to a specific activity exceeding 2000 IU/mg—data that supports use in inhibitor screening, IC50 determination, and kinetic parameter analysis including Km and kcat measurements. The absence of any fusion tag ensures the reactive center loop remains unobstructed, providing a suitable basis for substrate specificity profiling, drug candidate evaluation targeting serpinopathy-related conformational variants, and structural studies such as crystallography. Purity exceeding 95% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based functional assays and accurate enzymatic kinetic measurements.

Target Background

Function

Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator (Probable).

Gene References into Functions

We present two pediatric cases of progressive myoclonic epilepsy with SERPINI1 pathogenic variants that lead to a severe presentation. PMID: 28631894
Data indicated that rs9853967 and rs11714980 polymorphisms in CCM3 and SERPINI1respectively could be associated with a protective role in cerebral cavernous malformations disease. PMID: 27737651
SERPINI1 is an important regulator of epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer PMID: 26892864
The thermal and chemical stability along with the polymerisation propensity of both Wild Type and Glu289Ala NS were characterized. PMID: 26329378
This C-terminal lability is not required for neuroserpin polymerisation in the endoplasmic reticulum, but the additional glycan facilitates degradation of the mutant protein during proteasomal impairment. PMID: 26367528
the protective effect of neuroserpin maybe independent from its canonical interaction with a tissue-type plasminogen activator PMID: 26176694
Neuroserpin is expressed in naive effector memory and central memory CD4 and CD8 T cell subsets, and monocytes, B cells, and NK cells. T-cell activation caused 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
our 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 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 ischaemic 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
investigated the refolding and polymerization pathways of wild-type neuroserpin and of the pathogenic mutants S49P and H338R 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 physiologic effect of t-PA-NSP interactions may be more complex than previously thought. PMID: 12228252
Neuroserpin has a role as a selective inhibitor of tissue-type plasminogen activator in the central nervous system [review] PMID: 14983220
neuroserpin mutants that cause dementia accumulate as polymers within the endoplasmic reticulum PMID: 15090543
tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system PMID: 15269833
reactive centre loop of neuroserpin Portland being 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 so protects neurons in Alzheimer disease PMID: 16849336
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 PMID: 18051703
We report a neuroserpin mutation that causes electrical status epilepticus of slow-wave sleep. PMID: 18591508
Neuroserpin and tissue plasminogen activator are associated with amyloid-beta plaques in Alzheimer brain tissue. PMID: 19222708
Human neuroserpin: structure and time-dependent inhibition 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

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Involvement in disease

Encephalopathy, familial, with neuroserpin inclusion bodies (FENIB)

Subcellular Location

Secreted. Cytoplasmic vesicle, secretory vesicle lumen. Perikaryon.

Protein Families

Serpin family

Tissue Specificity

Detected in brain cortex and hippocampus pyramidal neurons (at protein level). Predominantly expressed in the brain.

Database Links

HGNC: 8943

OMIM: 602445

KEGG: hsa:5274

STRING: 9606.ENSP00000295777

UniGene: Hs.478153

Code	CSB-AP000141HU
Abbreviation	Recombinant Human SERPINI1 protein (Active)
MSDS	MSDS Datasheet
Size	$142
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Recombinant Human Neuroserpin protein (SERPINI1) (Active)

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