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Basic Info
CAS Number
NA
Pharmacopoeia
In-house Standards
Grade
pharmaceutical grade
Is Manufacturer
YES
Product Description
The recombinant aprotinin exhibits identical enzymatic properties to animal-derived aprotinin and can serve as a substitute for animal-sourced aprotinin in various biotechnological processes, such as: inhibiting serine protease activity during recombinant protein production, cell culture, and other applications.
AI Product Description
*The following content is generated by AI and is for reference only.
Aprotinin, also known as aprotinin or Trasylol, is a potent serine protease inhibitor derived from bovine lung tissue. Its molecular formula is C59H87N17O16S2, and it carries the CAS Registry Number 9087-70-1. This glycoprotein consists of a single polypeptide chain with approximately 58 amino acids, stabilized by three disulfide bonds that confer high structural stability against thermal denaturation and proteolytic degradation.
Historically, Aprotinin has been widely utilized in clinical settings to reduce perioperative bleeding during high-risk cardiac surgeries, such as coronary artery bypass grafting (CABG) and valve replacements. By inhibiting key enzymes like plasmin, kallikrein, trypsin, and chymotrypsin, it effectively suppresses fibrinolysis and attenuates the inflammatory response triggered by cardiopulmonary bypass. This mechanism significantly decreases blood loss, reduces the need for allogeneic blood transfusions, and lowers postoperative mortality rates in specific patient populations. Beyond surgery, it finds applications in laboratory research for preserving protein integrity during cell lysis and preventing enzymatic degradation in biochemical assays. It is frequently employed in the purification of recombinant proteins where protease activity must be strictly controlled.
Despite its efficacy, the use of Aprotinin has faced significant regulatory scrutiny due to safety concerns regarding renal failure and thrombotic events identified in large-scale studies around 2007. Consequently, its approval was suspended in many countries, including the European Union and the United States, though it remains available under strict restricted access programs or for compassionate use in life-threatening hemorrhage scenarios where no alternatives exist. Today, while synthetic inhibitors are often preferred, Aprotinin remains a benchmark molecule in protease inhibition studies. Its unique structure continues to inspire the development of novel therapeutic agents targeting coagulation and inflammation pathways. Researchers value it not only for its historical clinical impact but also as a critical tool for understanding complex proteolytic cascades in physiological and pathological conditions.
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