Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes with, and blocks the active sites of serine protease enzymes. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage.
It is used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.
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.
Grade: Cell Culture Reagent
Specific Activity: ~4 inhibitor u/mg
Suitability: Suitable for cell culture.
Key Applications: Serine protease inhibitor
Application Areas: Molecular Biology
Product Type: Biochemicals
Gene Id: Cow - 404172
Extinction Coefficient (E1%): E1% (280 nm) = 8.3 (water)(Lit.)
UV/Visible Absorbance: λ max (water) : 277 ± 5 nm
Presentation: White Powder
Format: Powder
Isoelectric point (pI): 10.5(Lit.)
pH: 5.0 - 7.0 (1% aq soln)
Water Content: <6%
Stability: Aprotinin is relatively stable to high temperature, acids, alkali, organic solvents and proteolytic digestion (only thermolysin has been found capable of degrading aprotinin after heating to 60-80°C). The Cyc14-Cys38 disulfide bridge is readily split by reducing agents like β-mercaptoethanol.
Solubility: Soluble in water (10 mg/mL - completely soluble) and in aqueous buffers of low ionic strengths.
Sterilization of Solutions: Sterilization of solutions can be done by filtration through a 0.2 µm filter.
Storage & Handling: Store at +4°C.