Aprotinin - CAS 9087-70-1
Catalog number:
9087-70-1
Category:
Inhibitor
Not Intended for Therapeutic Use. For research use only.
Molecular Formula:
C284H432N84O79S7
Molecular Weight:
6511.83
COA:
Inquire
Targets:
Ser/Thr Protease
Description:
Aprotinin is the small protein bovine pancreatic trypsin inhibitor (BPTI). It is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. It is a competitive serine protease inhibitor which blocks the active sites of enzyme by forming stable complexes with. It is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges. It is used as medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. It is used clinically to prevent postoperative blood loss and reduce transfusion requirements in those procedures which employ extracorporeal circulation. It is also used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest. It was temporarily withdrawn worldwide in 2007. It was reverted its previous standpoint regarding aprotinin by the European Medicines Agency (EMA) scientific committeeand in February 2012.
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Purity:
>98%
Appearance:
White or beige dry powder
Synonyms:
H-ARG-PRO-ASP-PHE-CYS-LEU-GLU-PRO-PRO-TYR-THR-GLY-PRO-CYS-LYS-ALA-ARG-ILE-ILE-ARG-TYR-PHE-TYR-ASN-ALA-LYS-ALA-GLY-LEU-CYS-GLN-THR-PHE-VAL-TYR-GLY-GLY-CYS-ARG-ALA-LYS-ARG-ASN-ASN-PHE-LYS-SER-ALA-GLU-ASP-CYS-MET-ARG-THR-CYS-GLY-GLY-ALA-OH;EC: 3.4.21.9;Iniprol;Trasylol;Trazinin;Zymofren;Riker 52G
Solubility:
H2O: > 10 mg/mL
Storage:
2-8ºC
MSDS:
Inquire
Application:
Aprotinin is used as medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. It is used clinically to prevent postoperative blood loss and reduce transfusion requirements in those procedures which employ extracorporeal circulation. It is also used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest.
Quality Standard:
In-house standard
Shelf Life:
2 month in rt, long time
Quantity:
Grams to Kilograms
InChIKey:
ZPNFWUPYTFPOJU-YSFZTAPISA-N
InChI:
InChI=1S/C284H432N84O79S7/c1-21-144(9)222-271(439)337-174(68-46-105-309-282(300)301)239(407)340-187(120-160-77-85-164(374)86-78-160)251(419)341-185(116-156-55-29-24-30-56-156)250(418)342-188(121-161-79-87-165(375)88-80-161)252(420)346-191(123-208(291)378)
Canonical SMILES:
CCC(C)C1C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NCC(=O)NC(C(=O)NC2CSSCC3C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(CSSCC(C(=O)NC(C(=O)NC(C(=O)N4CCCC4C(=O)N5CCCC5C(=O)NC(C(=O)NC(C(=O)NCC(=O)N6CCCC6C(=O)NC(CSSCC(C(=O)NC(C(=O)NC(C(=
1.A new anti-fibrinolytic hemostatic compound 8-O-acetyl shanzhiside methylester extracted from Lamiophlomis rotata.
Fan PC1, Ma HP1, Hao Y2, He XR2, Sun AJ1, Jiang W2, Li MX1, Jing LL1, He L2, Ma J3, Jia ZP4. J Ethnopharmacol. 2016 Apr 13. pii: S0378-8741(16)30206-9. doi: 10.1016/j.jep.2016.04.016. [Epub ahead of print]
BACKGROUND: Fibrinolysis prevents blood clots from growing and becoming problematic. Antifibrinolytics are used as inhibitors of fibrinolysis. Aprotinin was abandoned after identification of major side effects, especially on kidney. Lysine analogues has their own defects and whether they are adequate substitutes for aprotinin is still under doubt. Lamiophlomis rotata (Benth.) Kudo. was previous found to have hemostatic activity. But the active compound in L. rotata and its hemostatic mechanism were unknown.
2.Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri.
Silva MF1, Mota CM2, Miranda Vdos S3, Cunha Ade O4, Silva MC5, Naves KS6, de Oliveira F7,8, Silva DA9, Mineo TW10, Santiago FM11. Toxins (Basel). 2015 Nov 30;7(12):5114-28. doi: 10.3390/toxins7124869.
Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro, and defibrinating activity in vivo.
3.(99m) Tc-aprotinin - optimisation and validation of radiolabelling kits for routine preparation for diagnostic imaging of amyloidosis.
Denholt C1, Gillings N1. J Labelled Comp Radiopharm. 2016 Apr;59(4):171-4. doi: 10.1002/jlcr.3381. Epub 2016 Feb 28.
Technetium-99m aprotinin was prepared from an optimised radiolabelling kit formulation containing aprotinin, alkaline buffer and stannous chloride (reducing agent) and radiolabelled using (99m) Tc-pertechnetate. The labelling was achieved within 25 min, with radiochemical purities of >98%.
4.Contribution of the Kallikrein/Kinin System to the Mediation of ConA-Induced Inflammatory Ascites.
Baintner K1. Acta Microbiol Immunol Hung. 2016 Mar;63(1):131-7. doi: 10.1556/030.63.2016.1.10.
Intraperitoneal administration of concanavalin A (ConA, 25 mg/kg b.w.), a cell-binding plant lectin was used for inducing inflammatory ascites, and potential inhibitors were tested in 1 h and 2.5 h experiments, i.e. still before the major influx of leucocytes. At the end of the experiment the peritoneal fluid was collected and measured. The ConA-induced ascites was significantly (p<0.01) and dose-dependently inhibited by icatibant (HOE-140), a synthetic polypeptide antagonist of bradykinin receptors. Aprotinin, a kallikrein inhibitor protein also had significant (p<0.01), but less marked inhibitory effect. L-NAME, an inhibitor of NO synthesis, and atropine methylnitrate, an anticholinergic compound, were ineffective. It is concluded, that the kallikrein/kinin system contributes to the mediation of the ConA-induced ascites by increasing subperitoneal vascular permeability, independent of the eventual vasodilation produced by NO. It is known, that membrane glycoproteins are aggregated by the tetravalent ConA and the resulting distortion of membrane structure may explain the activation of the labile prekallikrein.
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CAS 9087-70-1 Aprotinin

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