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Recombinant Human Neuroserpin Protein, >95%(SDS-PAGE and HPLC), high purity

  • ActiBioPure™
  • Animal Free
  • Azide Free
  • Bioactive
  • Carrier Free
  • High performance
  • ≥95%(SDS-PAGE&HPLC)
Features and benefits
  • Expression System: E.coli
  • Accession #: Q99574
  • Protein Tag: No tag
  • Bioactivity: 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.
  • Endotoxin Concentration: <1 EU/μg
Item Number
rp149226
Grouped product items
SKUSizeAvailabilityPrice Qty
rp149226-10μg
10μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$69.90
rp149226-50μg
50μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$329.90
rp149226-100μg
100μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$599.90
rp149226-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,999.90

Animal Free, >95%(SDS-PAGE and HPLC), Active, E.coli, No tag, 17-410 aa

Basic Description

Product NameRecombinant Human Neuroserpin Protein, >95%(SDS-PAGE and HPLC), high purity
SynonymsDKFZp781N13156; 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 peptida
GradeActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, High performance
Product Description

Purity

> 95% by SDS-PAGE and HPLC analyses.


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.

Specifications & PurityActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE&HPLC)
Purity>95%(SDS-PAGE and HPLC)
BioactivityFully 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.
Endotoxin Concentration<1 EU/μg
Expression SystemE.coli
SpeciesHuman
Amino Acids17-410 aa
SequenceTGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EG
Protein TagNo tag
Protein LengthFull length protein
Accession #Q99574
SourceRecombinant
Predicted molecular weight44.7 kDa

Images

Recombinant Human Neuroserpin protein (rp149226)-Protein Bioactivity
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.

Recombinant Human Neuroserpin protein (rp149226)-SDS-PAGE
Recombinant Human Neuroserpin protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a single band at 44.7 kDa.

Product Specifications

FormLyophilized
ReconstitutionWe recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportio
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InDry ice
Stability And StorageUse a manual defrost freezer and avoid repeated freeze-thaw cycles.12 months from date of receipt, -20 to -70 °C as supplied.1 month, 2 to 8 °C under sterile conditions after reconstitution.3 months, -20 to -70 °C under sterile conditions after reconstitu

Certificates

Certificate of Analysis(COA)

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3 results found

Lot NumberCertificate TypeDateItem
ZJ23F0600451Certificate of AnalysisMar 26, 2024 rp149226
ZJ23F0600452Certificate of AnalysisMar 26, 2024 rp149226
ZJ23F0600453Certificate of AnalysisMar 26, 2024 rp149226

Related Documents

References

1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K et al..  (2004)  Complete sequencing and characterization of 21,243 full-length human cDNAs..  Nat Genet,  36  (1): (40-5).  [PMID:14702039]
2. Schrimpf, S P SP and 8 more authors..  (1997)  Human neuroserpin (PI12): cDNA cloning and chromosomal localization to 3q26..  Genomics,    (15):   [PMID:9070919]
3. Osterwalder, T T and 7 more authors..  (1998)  The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin..  The Journal of biological chemistry,    (23):   [PMID:9442076]
4. Davis, R L RL and 19 more authors..  (1999)  Familial dementia caused by polymerization of mutant neuroserpin..  Nature,    (23):   [PMID:10517635]
5. Belorgey, Didier D, Crowther, Damian C DC, Mahadeva, Ravi R and Lomas, David A DA..  (2002)  Mutant Neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro..  The Journal of biological chemistry,    (10):   [PMID:11880376]
6. Ishigami, Shoji S and 5 more authors..  (2007)  Identification of a novel targeting sequence for regulated secretion in the serine protease inhibitor neuroserpin..  The Biochemical journal,    (15):   [PMID:17040209]
7. Bechtel, Stephanie S and 18 more authors..  (2007)  The full-ORF clone resource of the German cDNA Consortium..  BMC genomics,    (31):   [PMID:17974005]
8. Ricagno, Stefano S, Caccia, Sonia S, Sorrentino, Graziella G, Antonini, Giovanni G and Bolognesi, Martino M..  (2009)  Human neuroserpin: structure and time-dependent inhibition..  Journal of molecular biology,    (24):   [PMID:19265707]
9. Takehara, Sayaka S and 6 more authors..  (2009)  The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability..  Journal of molecular biology,    (24):   [PMID:19285087]
10. Noto, Rosina R and 7 more authors..  (2015)  The stability and activity of human neuroserpin are modulated by a salt bridge that stabilises the reactive centre loop..  Scientific reports,    (2):   [PMID:26329378]

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