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Aprotinin is a serin protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Effective concentration equimolar to protease, normally 2-10µg/mL (about 1mM). Aprotinin is stable for long time at 4°C as lyophilised powder. It is also possible to store stock solutions for several years at -20°C. We recommend to prepare small samples as stock solutions, as repetitive freeze-thawing cycles as aggregation will occur after few thawing and freezing cycles.
Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.
purified inhibitor of Trypsin, Chymotrypsin, Plasmin and especially Kallikrein
Assay: min. 90.0 % (protein assay)
Acitivity: min. 5250 KIU/mg (>5.17 TIU/mg)
pH (1%, H2O) = 5.0 - 7.5
Water (K.F.): max. 6%
MW = 6511.52 g/mol.
activity conversions: >5250 KIU/mg; >5.17 TIU/mg; >2.58 PEU/mg
application:for in vitro inhibition of fibrinolytic activity in blood samples
Unit Definition:1 IU (inhibitor unit) inhibits 1 U trypsin as defined by cleavage of 1µmol BAEE (N-benzoyl-L-arginine ethyl ester) per minute. Activity in other units: min. 3 Ph. Eur. Units (PEU)/mg, based on dried substance. Unit definition: 1 Ph. Eur. Unit of aprotinin inhibits 50 % of the enzymatic activity of 2 microkatals trypsin, measured with BAEE as substrate at pH8.0 and 25°C. Activity in other units: min. 5850 Kallikrein Inactivator Units (KIU)/mg, based on dried substance. (KIU = PEU x 60 x 32.5).
Sicherheits Hinweise / SafetyH-Sätze: H317, H334
GHS-Symbole: GHS07, GHS08
Klassifizierungen / ClassificationEC-Nr: 232-994-9
Dokumente - Protokolle - Downloads
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