Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in 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).
Description: Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: The protein (1mg/ml) was lyophilized with no additives.
Solubility: It is recommended to reconstitute the lyophilized Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability: Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HAS or BSA). Please prevent freeze-thaw cycles.
Unit Definition:
1 Unit corresponds to 1 biological kallikrein inhibitor unit (KIU)
1 TIU =1,300 KIU.
Specific Activity: 6,438 KIU (Kallikrein Inactivator Units) per mg, 3.58 TIU/mg.
