Produkty
Producenci
APROTININ
Opis
Biochemical Physiological Actions
Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3. Effective concentration equimolar with protease.
| Source | Bovine Lung |
| Specific Activity | ≥3 TIU/mg |
| Typical Working Concentration | Equimolar with protease (1-2 ug/ml). |
| Unit Definition | One trypsin inhibitor unit (TIU), which is equal to 900 kallikrein inhibitor units (KIU) and 8,800 Schwert and Takenake units (STU), is the amount of inhibitor per mg which hydrolyzes one μmole of benzoyl-DL-arginine-p-nitroanilide (BAPNA) per minute. One TIU reduces the activity of two trypsin units by 50%. |
Application Notes
Aprotinin is used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones. Small amounts of aprotinin can be added to tubes of drawn blood to enable laboratory measurement of rapidly degraded proteins such as glucagon. It can be labelled with fluorescein isothiocyanate. The conjugate retains its antiproteolytic and carbohydrate-binding properties and has been used as a fluorescent histochemical reagent for staining glycoconjugates (mucosubstances) that are rich in uronic or sialic acids. In cell biology aprotinin is used as an enzyme inhibitor to prevent protein degradation during lysis or homogenization of cells and tissues.
Usage Statement
Unless specified otherwise, MP Biomedical's products are for research or further manufacturing use only, not for direct human use. For more information, please contact our customer service department.
Dane techniczne
| Opakowanie | 25 mg |