Aprotinin

Lee Biosolutions  bovine lung Aprotinin is used for the isolation of proteins as well as for biopharmaceutical downstream purification to inhibit undesired proteolytic activity of serine proteases such as trypsin, plasmin, trypsinogen, urokinase, chymotrypsin, kallikrein, elastase and others.

Custom preparations, technical support, bulk quantities and aliquoting available, email Info@leebio.com for more details.

The stability of the Aprotinin molecule is due to the 3 disulfide bonds linking the 6 cysteine members of the chain (Cys5-Cys55, Cys14-Cys38 and Cys30-Cys51). The lysine (15)-alanine (16) sequence on this strongly basic polypeptide represents the active center.

A single chain polypeptide isolated from bovine lung with antifibrinolytic and anti-inflammatory activities. As a broad-spectrum serine protease inhibitor, aprotinin bovine competitively and reversibly inhibits the activity of a number of different esterases and proteases, including trypsin, chymotrypsin, kallikrein, plasmin, tissue plasminogen activator, and tissue and leukocytic proteinases, resulting in attenuation of the systemic inflammatory response (SIR), fibrinolysis, and thrombin generation. This agent also inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. Bovine Aprotinin REF: National Cancer Society/bovine/aprotinin.