| SKU | Size | Availability | Price | 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
| Product Name | Recombinant Human Neuroserpin Protein, ＞95%(SDS-PAGE and HPLC), high purity |
|---|---|
| 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 | Ser |
| Grade | ActiBioPure™, 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 & Purity | ActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE&HPLC) |
| Purity | ＞95%(SDS-PAGE and HPLC) |
| 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 | <1.0 EU/μg |
| Expression System | E.coli |
| Species | Human |
| Amino Acids | 17-410 aa |
| Sequence | TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL |
| Protein Tag | No tag |
| Protein Length | Full length protein |
| Accession # | Q99574 |
| Source | Recombinant |
| Predicted molecular weight | 44.7 kDa |
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.
| Form | Lyophilized |
|---|---|
| Reconstitution | We 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 Temp | Store at -20°C,Avoid repeated freezing and thawing |
| Shipped In | Ice chest + Ice pads |
| Stability And Storage | Use 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 |
Enter Lot Number to search for COA:
Find and download the COA for your product by matching the lot number on the packaging.
| Lot Number | Certificate Type | Date | Item |
|---|---|---|---|
 ZJ23F0600451 | Certificate of Analysis | Mar 26, 2024 | rp149226 |
| ZJ23F0600452 | Certificate of Analysis | Mar 26, 2024 | rp149226 |
| ZJ23F0600453 | Certificate of Analysis | Mar 26, 2024 | rp149226 |
| 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] [10.1021/op500134e] |
| 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] |
