Synonyms Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Introduction Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
Description Aprotinin Bovine Recombinant is approximately 6,512 Dalton highly purified and designed specifically for cell culture applications, protein purification, diagnostic testing and pharmaceuticals.
It is produced without the use of animal- or human-derived materials and is therefore free from risk of contaminating human or animal-derived viruses or prions.
Source Maize (Corn).
Physical Appearance Sterile Filtered lyophilized powder.
Formulation The protein was lyophilized without any additives.
Solubility It is recommended to reconstitute the Aprotinin in sterile 18MO-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability Aprotinin although stable at room temperature for 3 weeks, should be stored at 4°C.
Purity Greater than 90.0% as determind by Gel Electrophoresis.
Activity 4.6 TIU/mg.
Unit Defenition One Trypsin Inhibitory Unit (TIU) is equal to the amount of inhibitor with the ability to inhibit two trypsin units by 50% where one trypsin unit will hydrolyze 1.0 mmole of N-alpha-benzoyl-DL-Arginine-p-Nitroanilide (BAPNA) per minute at pH 7.8 at 25°C.
Usage CHI's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.