616370-M

Aprotinin, Bovine Lung, Crystalline

Aprotinin, Bovine Lung, Crystalline, CAS 9087-70-1, is a competitive, reversible, heat- and acid-stable inhibitor of proteolytic and esterolytic activities.

• Synonyme(s) : Aprotinin, Bovine Lung, Crystalline, Pancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor
• Numéro CAS: 9087-70-1
• Numéro MDL: MFCD00130541
• Code UNSPSC : 12352202
• Nomenclature NACRES : NA.25

Propriétés

• Niveau de qualité: 200
• Pureté: ≥95% (gel filtration chromatography)
• Forme: crystalline solid
• Activité spécifique: ≥5500 KIU/mg dry wt
• Fabricant/nom de marque: Calbiochem^®
• Conditions de stockage: OK to freeze; desiccated (hygroscopic)
• Impuretés: ≤10 EU/mg endotoxin
• Couleur: white to off-white
• pl: 10.5
• Solubilité: water: 10 mg/mL
• Température de stockage: 2-8°C

Description

Description générale

A competitive and reversible inhibitor of esterase and protease activity. Forms a tight complex with and blocks the active site of target enzymes. Inhibits a number of different proteases, including chymotrypsin, coagulation factors involved in the pre-phase of blood clotting, kallikrein (K_d = 1 X 10^-7 M), plasmin (K_d = 2.3 X 10^-10 M), tissue and leukocyte proteinases, and trypsin (K_d = 5 X 10^-14 M). Does not inhibit Factor Xa or thrombin. Reported to be relatively acid and heat stable. Effectively inhibits target proteases at equimolar concentration. Useful as a serine proteinase inhibitor during purification of proteins and in studies of zymogen activation systems. Reported to suppress virus HA cleavage and limit reproduction of human and avian influenza viruses with a single arginine in the HA cleavage site.

A competitive and reversible inhibitor of esterases and proteases. Forms a tight complex with and blocks the active site of the enzymes. Inhibits a number of different proteases, including chymotrypsin, coagulation factors involved in the prephase of blood clotting, kallikrein (K_d = 1 x 10^-7 M), plasmin (K_d = 2.3 x 10^-10 M), tissue and leukocytic proteinases, and trypsin (K_d = 5 x 10^-14 M). Does not inhibit Factor Xa and thrombin. It is relatively acid- and heat-stable. Useful as a serine protease inhibitor during purification of proteins and in studies of zymogen activation systems. Reported to suppress virus HA cleavage and limit reproduction of human and avian influenza viruses with a single arginine in the HA cleavage site.

Effectively inhibits target proteases at equimolar concentration.

Note: 1 KIU = 0.025 antiplasmin units (APU) = 0.0016 trypsin inhibitor units (using porcine trypsin) = 0.0009756 trypsin inhibitor units (using bovine trypsin).

Actions biochimiques/physiologiques

Kd = 1 x 10-7 M, 2.3 x 10-10 M, 5 x 10-14 M, against kallikrein, plasmin, and trypsin, respectively

Primary Target
chymotrypsin

Avertissement

Toxicity: Standard Handling (A)

Définition de l'unité

One Kallikrein Inhibitory Unit (K.I.U.) is defined as the quantity of protease inhibitor that will inhibit two kallikrein units by 50% under optimal conditions. Note: 1 KIU = 0.025 antiplasmin units (APU) or 0.0031 trypsin inhibitor units.

Reconstitution

Following reconstitution refrigerate (4°C). Stock solutions are stable for up to 3 months at 4°C.

Autres remarques

Zhirnov, O.P., et al. 2011. Antiviral Res.92, 27.
Roberts, R.F., et al. 1998. Ann. Thorac. Surg.66, 225.
Azougagh Oualane, F., et al. 1992. Thromb. Res.68, 185.
Anderson, L.O., et al. 1986. Proc. Natl. Acad. Sci. USA83, 2979.
Kruithof, W.L., et al. 1986. Biochem. J.226, 631.
McKeehan, W.L., et al. 1986. J. Biol. Chem.261, 5378.
Fritz, H., and Wunderer, G. 1983. Arzneim. Forsch.33, 479.
Rijken, D.C., and Collen, D. 1981. J. Biol. Chem.256, 7035.
Kassell, B., et al. 1970. Methods Enzymol.19, 845.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Informations sur la sécurité

• Code de la classe de stockage: 11 - Combustible Solids
• Classe de danger pour l'eau (WGK): WGK 1
• Point d'éclair (°F): Not applicable
• Point d'éclair (°C): Not applicable