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Sigma-Aldrich

Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free

recombinant, expressed in Nicotiana, heat and acid-stable competitive, reversible inhibitor of serine proteases

Synonym(s):

Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free, Pancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor, Kallikrein-Trypsin Inactivator, Antikrein, Basic Pancreatic Trypsin Inhibitor

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About This Item

Empirical Formula (Hill Notation):
C284H432N84O79S7
CAS Number:
Molecular Weight:
6511.44
MDL number:
UNSPSC Code:
12352202
EC Index Number:
2329949
NACRES:
NA.77

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
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

Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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