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. 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. pH (5mg/ml): As Reported Activity: 4.7- 8.0 TIU/mg solid Protein: ~0.9mg protein/mg solid Loss on Drying: As Reported Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with terile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
