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Description: Aprotinin is a novel and potent small protein serine protease / bovine pancreatic trypsin inhibitor (BPTI) with antifibrinolytic activity. It inhibits trypsin and chymotrypsin with Kis of 0.06 pM and 9 nM, respectively. Aprotinin is used to reduce perioperative blood loss and transfusion. The use of aprotinin did not significantly increase the risk of renal failure or the need for postoperative renal replacement despite an increase in the proportion of patients who had a doubling of serum creatinine levels. The adjudication of death did not identify renal failure as contributing to or causing death associated with aprotinin use. A Meta analysis by Brown and colleagues showed a nonsignificant relative risk of renal failure with high-dose aprotinin.
References: J Mol Recognit. 1997 Jan-Feb;10(1):26-35; J Thromb Haemost. 2007 Oct;5(10):2113-8.
Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
This equation is commonly abbreviated as: C1V1 = C2V2
In vitro activity: Aprotinin is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. In cell biology, aprotinin is used as an enzyme inhibitor to prevent protein degradation during lysis or homogenization of cells and tissues. In the presence of aprotinin, the fibrinolytic activity is inhibited concentration dependently and the coagulation time is prolonged. Aprotinin is an effective inhibitor of the contact (intrinsic) coagulation pathway in vitro.
Cell Assay: Mouse G8-1 myoblasts are plated DMEM + 20% FBS (maintenance medium), in which they remain undifferentiated. When cells reach approximately 40-50% confluence, different protease inhibitors are added to the culture media and cells are incubated overnight. Cells are then switched to differentiation-promoting media (DMEM + 10% horse serum ± protease inhibitor) and incubated for 7 days.
Purity ≥98%
COA
MSDS