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CAS NO:
9087-70-1
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Basic Info
CAS Number
9087-70-1
Pharmacopoeia
ChP
Grade
In-house Standards
Is Manufacturer
YES
Packaging & Delivery
Minimum Order Quantity
Any
Delivery Cycle
Negotiable
Product Description
Reference Standards &Impurity
AI Product Description
*The following content is generated by AI and is for reference only.
Aprotinin, chemically known as aprotinin, is a potent serine protease inhibitor derived from bovine lung tissue. Its molecular formula is C59H93N17O16S2, and it carries the CAS registry number 9087-70-1. Structurally, this single-chain polypeptide consists of 58 amino acid residues with a molecular weight of approximately 6,512 Daltons. The molecule features three distinct disulfide bonds that stabilize its tertiary structure, enabling it to effectively bind and inhibit various serine proteases, including trypsin, chymotrypsin, plasmin, kallikrein, and cathepsin G.
Historically, Aprotinin has been widely utilized in clinical settings to reduce perioperative blood loss during high-risk surgeries, such as cardiac procedures involving cardiopulmonary bypass and major orthopedic operations. By inhibiting fibrinolysis and stabilizing endothelial barriers, it significantly decreases transfusion requirements and improves patient outcomes in specific surgical contexts. Beyond medicine, it serves as an essential research tool in biochemistry and cell biology laboratories for studying protein degradation pathways, enzyme kinetics, and protease functions. Researchers often employ it to preserve sample integrity during protein extraction and purification processes, preventing unwanted enzymatic cleavage.
Despite its therapeutic efficacy, the use of Aprotinin has faced regulatory scrutiny due to safety concerns regarding thrombotic events and renal complications identified in large-scale studies. Consequently, its availability varies by region, with some markets restricting its indication to life-threatening hemorrhage cases where alternative treatments are ineffective. Nevertheless, it remains a critical reagent in scientific research for understanding proteolytic mechanisms. The compound is typically supplied as a sterile lyophilized powder or solution, requiring careful storage at controlled temperatures to maintain stability. Its unique mechanism of action continues to inspire the development of next-generation protease inhibitors with improved safety profiles, highlighting its enduring significance in both pharmaceutical science and biomedical research.
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