Recombinant Human Neuroserpin protein(SERPINI1) (Active)

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Code CSB-AP000141HU
Size US$3274Purchase it in Cusabio online store
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Product Details

Purity >95% as determined by SDS-PAGE and HPLC.
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 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 Basically, we can dispatch the products out in 5-10 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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.

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Target Data

Function Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin
Gene References into Functions
  1. We present two pediatric cases of progressive myoclonic epilepsy with SERPINI1 pathogenic variants that lead to a severe presentation. PMID: 28631894
  2. 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
  3. SERPINI1 is an important regulator of epithelial-mesenchymal transition in an orthotopic implantation model of colorectal cancer PMID: 26892864
  4. The thermal and chemical stability along with the polymerisation propensity of both Wild Type and Glu289Ala NS were characterized. PMID: 26329378
  5. 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
  6. the protective effect of neuroserpin maybe independent from its canonical interaction with a tissue-type plasminogen activator PMID: 26176694
  7. 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
  8. Molecular Dynamics simulations suggest that Neuroserpin conformational stability and flexibility arise from a spatial distribution of intramolecular salt-bridges and hydrogen bonds. PMID: 25450507
  9. Alzheimer's disease brain tissues with elevated neuroserpin protein also showed increased expression of THRbeta1 and HuD PMID: 24036060
  10. our study did not provide any evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke PMID: 21487809
  11. the origins of conformational lability PMID: 21961602
  12. 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
  13. Hrd1 and gp78 mediate mutant neuroserpin turnover through the ERAD pathway. PMID: 21507957
  14. 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
  15. 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
  16. investigated the refolding and polymerization pathways of wild-type neuroserpin and of the pathogenic mutants S49P and H338R PMID: 20691191
  17. Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro PMID: 11880376
  18. 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
  19. Neuroserpin has a role as a selective inhibitor of tissue-type plasminogen activator in the central nervous system [review] PMID: 14983220
  20. neuroserpin mutants that cause dementia accumulate as polymers within the endoplasmic reticulum PMID: 15090543
  21. tissue plasminogen activator and neuroserpin are widely expressed in the human central nervous system PMID: 15269833
  22. 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
  23. 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
  24. neuroserpin interacts with Abeta(1-42) to form off-pathway non-toxic oligomers and so protects neurons in Alzheimer disease PMID: 16849336
  25. intergenic region of the head-to-head PDCD10-SERPINI1 gene pair provides an interesting and informative example of a complex regulatory system PMID: 17212813
  26. in a French family with the S52R mutation of the neuroserpin gene, progressive myoclonic epilepsy was associated with a frontal syndrome PMID: 17606885
  27. This study provides the first evidence that neuroserpin is associated with early-onset ischemic stroke among Caucasian women. PMID: 17961231
  28. conformational modification in the protein under oxidative stress PMID: 18051703
  29. We report a neuroserpin mutation that causes electrical status epilepticus of slow-wave sleep. PMID: 18591508
  30. Neuroserpin and tissue plasminogen activator are associated with amyloid-beta plaques in Alzheimer brain tissue. PMID: 19222708
  31. Human neuroserpin: structure and time-dependent inhibition PMID: 19265707
  32. Analyses restricted to glioblastoma (n = 254) yielded significant associations for the SELP, DEFB126/127, SERPINI1, and LY96 genetic regions. PMID: 19423540
  33. 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) (PubMed:17040209). Predominantly expressed in the brain (PubMed:9070919).
Database Links

HGNC: 8943

OMIM: 602445

KEGG: hsa:5274

STRING: 9606.ENSP00000295777

UniGene: Hs.478153

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