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9087-70-1 Usage


Aprotinin, also known as pancreatic trypsin inhibitor (BPTI), is a potent protease inhibitor derived from bovine lung. It is a reversible inhibitor of serine proteases such as trypsin, chymotrypsin, and kallikrein, and is also a weaker inhibitor of thrombin and trypsinogen. Aprotinin is found in various organs including lungs, spleen, liver, and pancreas, and is present in the free form in calf serum. It is a white powder and is marketed under the brand name Trasylol by Bayer.


Used in Biochemistry Research:
Aprotinin is used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones, helping to prevent the degradation of proteins of interest during the analysis process.
Used in Enzyme Purification:
Aprotinin is involved in the purification of urokinase, trypsin, and chymotrypsin on immobilized aprotinin, serving as a crucial tool in the separation and isolation of these enzymes.
Used in Quantification of Kallikrein Activity:
Aprotinin is utilized in the quantification of kallikrein activity in mixtures of esterases and proteases, providing a means to measure the activity of this enzyme accurately.
Used in Protein Purification:
Aprotinin is widely used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest, ensuring the integrity of the target protein during purification processes.
Used in Pharmaceutical Industry:
Aprotinin acts as a reversible serine protease blocking and binding agent, and is widely employed as an inhibitor of trypsin, making it a valuable component in the development of drugs targeting protease-related conditions.
Used in Clinical Applications:
Although not explicitly mentioned in the provided materials, Aprotinin has been used clinically to reduce bleeding and the need for blood transfusions in cardiac surgery patients, highlighting its potential therapeutic applications. However, it is important to note that the clinical use of Aprotinin has been a subject of debate due to safety concerns, and its use may be restricted or discontinued in some regions.



Manufacturing Process

1 kg of parotid of cattle, which were freed of fat and flesh are comminuted in a meat chopper and twice extracted with 5 L of acetone. The acetone was removed as far as possible by sucking off and the moist material is digested for 2.5 hours in 1.2 L of 1 N acetic acid and 2.8 L of 96% ethanol at 50°C. The filtrate containts about 230.000 inactivator units. The alcoholic solution is concentrated to 1.2 L by evaporating in vacuo and shaken with an equal amount of ether. Dark coloring matters and residues of fat are thus dissolved. The aqueous phase is now mixed with acetone until a precipitate occurs and the dissolved in dilute acetic acid. The solution is brought to a weakly alkaline pH by addition of ammonia. It is then centrifuged and the inactivator is precipitated with five times the amount of ethanol. The yield amounts to about 180.000 kallikrein inactivator units in 0.4-0.5 g of substance.

Therapeutic Function

Proteinase inhibitor

Biochem/physiol Actions

Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin 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.

Safety Profile

Experimental reproductive effects. When heated to decomposition it emits toxic fumes of NOx and SOx.


1. henry da, carless pa, moxey aj, et al. anti-fibrinolytic use for minimising perioperative allogeneic blood transfusion. cochrane database syst rev 2007; 4: cd001886.2. levi m, cromheecke me, de jonge e, et al. pharmacological strategies to decrease excessive blood loss in cardiac surgery: a meta-analysis of clinically relevant endpoints. lancet 1999; 354: 1940-7.3. sedrakyan a, treasure t, elefteriades ja. effect of aprotinin on clinical outcomes in coronary artery bypass graft surgery: a systematic review and meta-analysis of randomized

Check Digit Verification of cas no

The CAS Registry Mumber 9087-70-1 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,8 and 7 respectively; the second part has 2 digits, 7 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 9087-70:
121 % 10 = 1
So 9087-70-1 is a valid CAS Registry Number.

9087-70-1 Well-known Company Product Price

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  • (Code)Product description
  • CAS number
  • Packaging
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  • Sigma-Aldrich

  • (Y0001154)  Aprotinin for system suitability  European Pharmacopoeia (EP) Reference Standard

  • 9087-70-1

  • Y0001154

  • 1,880.19CNY

  • Detail
  • Sigma-Aldrich

  • (A1250000)  Aprotininsolution  BRP, European Pharmacopoeia (EP) Reference Standard

  • 9087-70-1

  • A1250000

  • 1,880.19CNY

  • Detail



According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017


1.1 GHS Product identifier

Product name Aprotinin

1.2 Other means of identification

Product number -
Other names cas9004-04-0

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:9087-70-1 SDS

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