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Key Documents

616370-M

Sigma-Aldrich

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.

Sinónimos:

Aprotinin, Bovine Lung, Crystalline, Pancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.25

Quality Level

assay

≥95% (gel filtration chromatography)

form

crystalline solid

specific activity

≥5500 KIU/mg dry wt

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)

impurities

≤10 EU/mg endotoxin

color

white to off-white

pI 

10.5

solubility

water: 10 mg/mL

storage temp.

2-8°C

General description

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 (Kd = 1 X 10-7 M), plasmin (Kd = 2.3 X 10-10 M), tissue and leukocyte proteinases, and trypsin (Kd = 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 (Kd = 1 x 10-7 M), plasmin (Kd = 2.3 x 10-10 M), tissue and leukocytic proteinases, and trypsin (Kd = 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).

Biochem/physiol Actions

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

Warning

Toxicity: Standard Handling (A)

Unit Definition

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.

Other Notes

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.

Legal Information

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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