Bovine Aprotinin / Pancreatic Trypsin Inhibitor

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Product Overview, Sizes and Prices



Synonyms: Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

Source: Bovine Lung

Biological activity: 3,5 PEU (Ph. Eur. Units)/mg; 6300 KIU (Kallikrein Inactivator Units)/mg

Physical state: Lyophilized

Manufacturer:  Active Bioscience

Article No. Size Price  
1155.919.166 100 mg 195 €
1155.919.258 250 mg 330 €
1155.919.188 1 g 990 €

Please inquire for other vial sizes and custom vialing.



Product Details


Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.


Description of Bovine Aprotinin / Pancreatic Trypsin Inhibitor

Aprotinin/Pancreatic Trypsin Inhibitor is a natural proteinase inhibitor polypeptide consisting of 58 amino acids with a molecular mass of 6,5 kDa It is a single polypeptide chain which is cross-linked by three disulfide bridges. Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g. GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g. CD11b). It can be used for in vitro inhibition of fibrinolytic activity in blood samples.



Aprotinin is used for the protection of proteins and enzymes during isolation/purification. Inhibition of protease activity increases cell longevity in cell and tissue culture studies. Purification of urokinase, trypsin and chymotrypsin on immobilized aprotinin. Quantification of kallikrein activity in mixtures of esterases and proteases. Controlled degradation of substrates by avoiding nonspecific proteolysis in clinical chemistry assays. Aprotinin is a model protein for protein folding studies. Molecular mass marker in SDS-polyacrylamide gel electrophoresis.


Definition of the units

1 Ph. Eur.-unit of Aprotinin inhibits 50 % of the enzymatic activity of 2 Microkatal Trypsin, with BAEE as Substrate, measured at pH 8,0 und 25 C.
1 PEU = 1800 KIU.



We recommend a quick spin followed by reconstitution in water to a concentration of at least 100 g/ml, which can then be further diluted. Do not vortex. This solution can be stored at 2-8C for up to 1 week or in working aliquots at -15C to -25C. Working aliquots should be at the highest practical concentration. For long term storage we recommend to add at least 0.1% BSA (order number: or HSA. Please avoid repeated freeze thaw cycles and contact with strongly basic solutions, inactive at pH > 12,8. Common working concentrations are between 0,06 and 2g/ml.



The lyophilized protein is stable at room temperature for up to 1 month and at least until the lot specific expiry date if kept below -18C. Reconstituted Aprotinin should be stored in working aliquots at -20C to -80C if possible with carrier protein, e.g. 0,1% BSA Please avoid repeated freeze-thaw cycles.


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