Aprotinin
Based on 31 publication(s) in Google Scholar
Aprotinin is a bovine pancreatic trypsin inhibitor (BPTI) inhibitor which inhibits trypsin and chymotrypsin with Kis of 0.06 pM and 9 nM, respectively.
Para uso exclusivo en investigación. No vendemos a pacientes.
- Pureza: 99.01%
- No. CAS: 9087-70-1
- Fòrmula: C284H432N84O79S7
- Peso molecular:6511.44
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Almacenamiento:
Please store the product under the recommended conditions in the Certificate of Analysis.
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Actividad biológica
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Chemical Information
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Solvente y solubilidad
- Protocolo
- Pureza y Documentación
- Referencias
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Help & FAQs
Publications Citing Use of MedChemExpress (MCE) Aprotinin
More- Nature. 2024 Aug;632(8025):686-694. [Abstract]
- Nature. 2024 Aug;632(8026):930-937. [Abstract]
- Cell. 2025 Nov 26;188(24):6861-6872.e14. [Abstract]
- Cell Res. 2025 May;35(5):385-388. [Abstract]
- Cell Res. 2025 Mar;35(3):165-185. [Abstract]
- Nat Commun. 2025 Jul 16;16(1):6551. [Abstract]
- Nat Commun. 2025 Apr 2;16(1):3153. [Abstract]
- Nat Commun. 2025 Mar 11;16(1):2412. [Abstract]
- Nat Commun. 2024 Jun 12;15(1):5039. [Abstract]
- Nat Commun. 2023 Jul 26;14(1):4487. [Abstract]
- Nat Commun. 2023 May 2;14(1):2523. [Abstract]
- Autophagy. 2024 Oct;20(10):2221-2237. [Abstract]
- Sci Adv. 2026 Jan 30;12(5):eadz8234. [Abstract]
- Proc Natl Acad Sci U S A. 2025 Dec 2;122(48):e2506722122. [Abstract]
- Proc Natl Acad Sci U S A. 2022 Jul 26;119(30):e2208211119. [Abstract]
- Food Res Int. 2025 Dec 29;227:118193.
- Cell Rep. 2025 Jan 15;44(1):115219. [Abstract]
- Cell Rep. 2024 Mar 27;43(4):114002. [Abstract]
- Cell Rep. 2021 Nov 2;37(5):109931. [Abstract]
- Biochem Pharmacol. 2025 Apr 23:237:116955. [Abstract]
- Int J Oncol. 2019 Jul;55(1):331-339. [Abstract]
- Am J Physiol Cell Physiol. 2017 Dec 1;313(6):C632-C643. [Abstract]
- Structure. 2025 Dec 4;33(12):2049-2057.e5. [Abstract]
- Sci Rep. 2025 May 6;15(1):15762. [Abstract]
- J Virol. 2023 May 31;97(5):e0032423. [Abstract]
- Biochim Biophys Acta Mol Cell Biol Lipids. 2025 Apr 26:159618. [Abstract]
- STAR Protoc. 2025 Jul 18;6(3):103963. [Abstract]
- STAR Protoc. 2023 Jun 28;4(3):102371. [Abstract]
- bioRxiv. 2025 Aug 20.
- bioRxiv. 2024 November 14.
- bioRxiv. 2023 Nov 5.
Customer Validation & Images
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WB
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WB
Actividad biológica
Ki: 0.06 pM (Trypsin), 9 nM (Chymotrypsin)[1]
Aprotinin, a serine protease inhibitor isolated from bovine lung, is a complex protease inhibitor that is an antifibrinolytic, inhibits contact activation, and decreases the inflammatory response to cardiopulmonary bypass[2]. Aprotinin inhibits trypsin (bovine, Ki= 0.06 pM), chymotrypsin (bovine, Ki= 9 nM), plasmin (human, 0.23 nM)[1]. Aprotinin is also a competitive protein inhibitor of NOS activity. It inhibits NOS-I and NOS-II with Ki values of 50 μM and 78 μM, respectively[3]. Aprotinin significantly inhibits fibrinolysis with an IC50 of 0.16±0.05 μM[4].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
| NCT Number | Sponsor | Condition | Start Date |
Phase
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|---|---|---|---|---|
| NCT01329991 | Plexxikon| | 2011-05 | PHASE1 |
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(Disulfide bridge: Cys5-Cys55,Cys14-Cys38,Cys30-Cys51)
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA(Disulfide bridge: Cys5-Cys55,Cys14-Cys38,Cys30-Cys51)
Chemical Information
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No. CAS 9087-70-1
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Appearance Solid
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Peso molecular 6511.44
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Fòrmula C284H432N84O79S7
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Color Off-white to light brown
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SMILES
O=C(N1[C@@H](CCC1)C(N[C@@H](CC(O)=O)C(N[C@@H](CC2=CC=CC=C2)C(N[C@@H](CSSC[C@@H](C(NCC(NCC(N[C@@H](C)C(O)=O)=O)=O)=O)NC3=O)C(N[C@@H](CC(C)C)C(N[C@@H](CCC(O)=O)C(N4[C@@H](CCC4)C(N5[C@@H](CCC5)C(N[C@@H](CC6=CC=C(C=C6)O)C(N[C@@H]([C@H](O)C)C(NCC(N7[C@@H](CCC7)C(N[C@@H](CSSC[C@@H](C(N[C@H](CCCNC(N)=N)C(N[C@@H](C)C(N[C@@H](CCCCN)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC(N)=O)C(N[C@@H](CC(N)=O)C(N[C@@H](CC8=CC=CC=C8)C(N[C@@H](CCCCN)C(N[C@@H](CO)C(N[C@@H](C)C(N[C@@H](CCC(O)=O)C(N[C@H]9CC(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)NC%10=O)C(N[C@@H](CCCCN)C(N[C@@H](C)C(N[C@@H](CCCNC(N)=N)C(N[C@@H]([C@@H](C)CC)C(N[C@@H]([C@@H](C)CC)C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CC%11=CC=C(C=C%11)O)C(N[C@@H](CC%12=CC=CC=C%12)C(N[C@@H](CC%13=CC=C(C=C%13)O)C(N[C@@H](CC(N)=O)C(N[C@@H](C)C(N[C@@H](CCCCN)C(N[C@@H](C)C(NCC(N[C@@H](CC(C)C)C(N[C@@H](CSSC[C@@H](C(N[C@@H](CCSC)C(N[C@@H](CCCNC(N)=N)C(N[C@H]3[C@H](O)C)=O)=O)=O)NC9=O)C(N[C@@H](CCC(N)=O)C(N[C@@H]([C@H](O)C)C(N[C@@H](CC%14=CC=CC=C%14)C(N[C@@H](C(C)C)C(N[C@@H](CC%15=CC=C(C=C%15)O)C(NCC(NC%10)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)[C@H](CCCNC(N)=N)N
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Structure Classification
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Initial Source
Bovine lung
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Envío
Room temperature in continental US; may vary elsewhere.
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Almacenamiento
Please store the product under the recommended conditions in the Certificate of Analysis.
Publications (31)
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Journal Impact Factor
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Most Recent
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Nature
2024 Aug;632(8025):686-694. PMID: 39112701 -
Nature
2024 Aug;632(8026):930-937. PMID: 39085602 -
Cell
2025 Nov 26;188(24):6861-6872.e14. PMID: 41138730 -
Cell Res
Structural basis of augmenting taurine uptake by the taurine transporter in alleviating cellular senescence. [Abstract]2025 May;35(5):385-388. PMID: 40108449 -
Cell Res
2025 Mar;35(3):165-185. PMID: 39875551 -
Nat Commun
2025 Jul 16;16(1):6551. PMID: 40670375 -
Nat Commun
Molecular insights into the α6β4 nicotinic acetylcholine receptor function and ligand recognition. [Abstract]2025 Apr 2;16(1):3153. PMID: 40175361 -
Nat Commun
2025 Mar 11;16(1):2412. PMID: 40069141 -
Nat Commun
2024 Jun 12;15(1):5039. PMID: 38866775 -
Nat Commun
Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis. [Abstract]2023 Jul 26;14(1):4487. PMID: 37495621 -
Nat Commun
Reduced hepatic bradykinin degradation accounts for cold-induced BAT thermogenesis and WAT browning in male mice. [Abstract]2023 May 2;14(1):2523. PMID: 37130842 -
Autophagy
PLK2-mediated phosphorylation of SQSTM1 S349 promotes aggregation of polyubiquitinated proteins upon proteasomal dysfunction. [Abstract]2024 Oct;20(10):2221-2237. PMID: 39316746 -
Sci Adv
Structural insight into the glucose-6-phosphate transport by G6PT1 and inhibition mechanism of CGA. [Abstract]2026 Jan 30;12(5):eadz8234. PMID: 41616054 -
Proc Natl Acad Sci U S A
2025 Dec 2;122(48):e2506722122. PMID: 41284875 -
Proc Natl Acad Sci U S A
Structural basis for high-voltage activation and subtype-specific inhibition of human Nav1.8. [Abstract]2022 Jul 26;119(30):e2208211119. PMID: 35858452 -
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Cell Rep
Menin orchestrates macrophage reprogramming to maintain the pulmonary immune homeostasis. [Abstract]2025 Jan 15;44(1):115219. PMID: 39817905 -
Cell Rep
Endocytic activation and exosomal secretion of matriptase stimulate the second wave of EGF signaling to promote skin and breast cancer invasion. [Abstract]2024 Mar 27;43(4):114002. PMID: 38547126
Aprotinin purchased from MedChemExpress. Usage Cited in: Cell Rep. 2024 Mar 27;43(4):114002. [Abstract]
A431 cells were treated with EGF (10 ng/mL) together with Aprotinin (2 μM) for 1 h. Proteins were detected by western blots.
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Cell Rep
2021 Nov 2;37(5):109931. PMID: 34731621 -
Biochem Pharmacol
GSNO induced mitochondrial Cx43 nitrosylation in cardiomyocyte differentiation from mouse ES cells in vitro. [Abstract]2025 Apr 23:237:116955. PMID: 40280246 -
Int J Oncol
Metformin induces TPC-1 cell apoptosis through endoplasmic reticulum stress-associated pathways in vitro and in vivo. [Abstract]2019 Jul;55(1):331-339. PMID: 31180536 -
Am J Physiol Cell Physiol
(Pro)renin receptor mediates albumin-induced cellular responses: role of site-1 protease-derived soluble (pro)renin receptor in renal epithelial cells. [Abstract]2017 Dec 1;313(6):C632-C643. PMID: 28903918
Aprotinin purchased from MedChemExpress. Usage Cited in: Am J Physiol Cell Physiol. 2017 Dec 1;313(6):C632-C643. [Abstract]
Effects of protease inhibitor PIC, a serine protease inhibitor AEBSF and trypsin and chymotrypsin inhibitors Aprotinin (Aprot, 0.1 mM) on PRR cleavage induced by BSA in HK-2 cells.
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Structure
2025 Dec 4;33(12):2049-2057.e5. PMID: 40914153 -
Sci Rep
Pharmacological alternatives to oxytetracycline as potential treatment of flexural limb deformities in foals: a preliminary in vitro cell viability and proliferation study. [Abstract]2025 May 6;15(1):15762. PMID: 40328831 -
J Virol
Identification of Embryonic Chicken Proteases Activating Newcastle Disease Virus and Their Roles in the Pathogenicity of Virus Used as In Ovo Vaccine. [Abstract]2023 May 31;97(5):e0032423. PMID: 37042750 -
Biochim Biophys Acta Mol Cell Biol Lipids
2025 Apr 26:159618. PMID: 40294697 -
STAR Protoc
Protocol for reconstituting enzymatic activities for ultra-large histone methyltransferases NSD1 and SETD2 using a baculovirus expression system. [Abstract]2025 Jul 18;6(3):103963. PMID: 40684435 -
STAR Protoc
2023 Jun 28;4(3):102371. PMID: 37384522 -
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Solvente y solubilidad
H2O : 100 mg/mL (15.36 mM; Need ultrasonic)
* Note: If you choose water as the stock solution, please dilute it to the working solution, then filter and sterilize it with a 0.22 μm filter before use.
* Note: If you choose water as the stock solution, please dilute it to the working solution, then filter and sterilize it with a 0.22 μm filter before use.
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
For the following dissolution methods, please prepare the working solution directly:
It is recommended to prepare fresh solutions and use them promptly within a short period of time.
The percentages shown for the solvents indicate their volumetric ratio in the final prepared solution. If precipitation or phase separation occurs during preparation, heat and/or sonication can be used to aid dissolution.
Add each solvent one by one: PBS
Solubility: 50 mg/mL (7.68 mM); Clear solution; Need ultrasonic
Please enter the basic information of animal experiments:
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Recommended: Prepare an additional quantity of animals to account for potential losses during experiments.
Working solution concentration: 0.22 mg/mL
This product has good water solubility, please refer to the measured solubility data in water/PBS/Saline for details.
Protocolo
Rats: Male Wistar rats (180-220 g) are used in the study. Aprotinin is dissolved in physiological saline. Aprotinin is administered by bolus injection followed by a maintenance infusion. The doses given are 1.5 mg kg-1 and 3 mg kg-1 h-1, 3mg kg-1 and 6 mg kg-1 h-1 up to 5 mg kg-1 and 10 mg kg-1 h-1. Plasma concentrations for the two agents are assessed by pharmacokinetic studies in rats[4].
Mice: An intact mouse model of ischemia/reperfusion (30 min-I/60 min-R) is used and left ventricular peak + dP/dt is measured in wild type mice (WT, C57BL/6; n=10), WT mice with aprotinin (4mL/kg; n=10), transgenic mice devoid of the TNFRI (TNFRInull; n=10), and TNFRInull with aprotinin (n=10)[6].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Pureza y Documentación
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Ficha de datos (313 KB)
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SDS (393 KB)
- English - EN (393 KB)
- Français - FR (393 KB)
- Deutsch - DE (393 KB)
- Norwegian - NO (393 KB)
- Español - ES (393 KB)
- Swedish - SV (393 KB)
- Italian - IT (393 KB)
- Portuguese - PT (393 KB)
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Instrucciones de manejo (2659 KB)
Referencias
[1]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62. [Content Brief]
[2]. Fritz H, et al. Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittelforschung. 1983;33(4):479-94. [Content Brief]
[4]. Venturini G, et al. Aprotinin, the first competitive protein inhibitor of NOS activity. Biochem Biophys Res Commun. 1998 Aug 10;249(1):263-5 [Content Brief]
[5]. Sperzel M, et al. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost. 2007 Oct;5(10):2113-8. Epub 2007 Jul 31. [Content Brief]
[6]. Davis R, et al. Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated withcardiac surgery. Drugs. 1995 Jun;49(6):954-83. [Content Brief]
[7]. Sabbagh MJ, et al. Aprotinin exacerbates left ventricular dysfunction after ischemia/reperfusion in mice lacking tumor necrosis factor receptor I. J Cardiovasc Pharmacol. 2008 Oct;52(4):355-62. [Content Brief]
Complete Stock Solution Preparation Table
| Optional Solvent | Concentration Solvent Mass | 1 mg | 5 mg | 10 mg | 25 mg |
|---|---|---|---|---|---|
| H2O | 1 mM | 0.1536 mL | 0.7679 mL | 1.5358 mL | 3.8394 mL |
| 5 mM | 0.0307 mL | 0.1536 mL | 0.3072 mL | 0.7679 mL | |
| 10 mM | 0.0154 mL | 0.0768 mL | 0.1536 mL | 0.3839 mL | |
| 15 mM | 0.0102 mL | 0.0512 mL | 0.1024 mL | 0.2560 mL |
* Note: If you choose water as the stock solution, please dilute it to the working solution, then filter and sterilize it with a 0.22 μm filter before use.
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