616371
Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free
recombinant, expressed in Nicotiana, heat and acid-stable competitive, reversible inhibitor of serine proteases
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Synonym(s):
Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free, Pancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor, Kallikrein-Trypsin Inactivator, Antikrein, Basic Pancreatic Trypsin Inhibitor
Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
MDL number:
UNSPSC Code:
12352200
EC Index Number:
2329949
NACRES:
NA.77
Recommended Products
recombinant
expressed in Nicotiana
Quality Level
Assay
≥98% (SDS-PAGE)
form
powder
specific activity
≥5.0 units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
color
white to off-white
shipped in
wet ice
storage temp.
2-8°C
General description
Recombinant, bovine aprotinin supplied without animal-derived components. Aprotinin is a competitive, reversible inhibitor of proteolytic and esterolytic activity. A relatively heat- and acid-stable serine protease inhibitor. Forms a tight complex, blocking the active site of the enzyme. Effective at concentrations equimolar with protease. Inhibits several proteases, including coagulation factors in the prephase of blood clotting, tissue and leukocytic proteinases, chymotrypsin, trypsin (Kd = 5 x 10-14 M), plasmin (Kd = 2.3 x 10-10 M), and kallikrein (Kd = 1 x 10-7 M). Proteases not inhibited by aprotinin include Factor Xa, thrombin, pepsin, papain, and carboxypeptidases A and B. Useful for protein purification and for extending the life of cells in culture by preventing proteolytic damage.
Biochem/physiol Actions
Cell permeable: no
Kd = 5 x 10-14 M, 2.3 x 10-10 M, 1 x 10-7 M against trypsin, plasmin, and kallikrein, respectively
Primary Target
chymotrypsin
chymotrypsin
Product does not compete with ATP.
Reversible: yes
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Standard Handling (A)
Unit Definition
One TIU (Trypsin Inhibitory Unit) will decrease the activity of two trypsin units by 50% where one trypsin unit will hydrolyze 1.0 µmole of Nα-benzoyl-L-Arginine-p-Nitroanilide (L-BAPNA) per minute at pH 7.8 at 25°C.
Physical form
Contains no animal-derived components.
Other Notes
Deutscher, M.P., 1990. Methods Enzymol.182, 83.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
nwg
Certificates of Analysis (COA)
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