Aprotinin Concentrated Solution

Aprotinin a single chain polypeptide of 58 amino-acid residues having a molecular weight of 6512.

Aprotinin is a broad-spectrum serine protease inhibitor of multiple proteolytic enzymes, specifically trypsin- or chymotrypsin-like proteases. It additionally offers anti-inflammatory activities.

Aprotinin inhibits serine proteases with various physiological functions. Important typical proteases inhibited by Aprotinin include trypsin, chymotrypsin, kallikreins and plasmin. It additionally weakly inhibits t-PA or u-PA (plasminogen activators), acrosin (essential for conception), human leukocyte elastase (inflammation), and activated protein C (thrombosis).

APPLICATION:
Aprotinin can be used to explore a potential contamination of biologicals with serine proteases e.g. kallikrein-like activity in cell culture, plasma fractions, factor concentrates etc. No effect in increasing aprotinin dose = no influence of proteases that are inhibited by Aprotinin. Aprotinin can also be employed effectively to make assays more specific, and it protects proteins involved in the assay, e.g. labile coagulation factors or fibrinogen.

Additionally, Aprotinin prevents unspecific cleavage of synthetic peptide substrates in chromogenic, amperometric, fluorogenic or luminogenic assays by contaminating proteases or their complexes with 2-macroglobulin. It also protects proteins measure in immunoassays against proteolysis, thus maintaining their integrity.

In cell culture media, Aprotinin inhibits degradation of proteohormones, cytokines or other important proteins. It can also extend the life span of certain cells in culture. Finally, injection of Aprotinin into lab animals may allow characterization of biochemical pathways which are the subject of proteolysis.

MODE OF ACTION:
As a competitive inhibitor, aprotinin forms a stable non–covalent complex with serine proteases and blocks their active centers in a reversible manner. Binding to serine proteases can be reversed in alkaline (pH 10) and acid environments (pH 5 for most proteases, pH <3 for trypsin and plasmin). At these extreme pH values, it should therefore be possible to separate aprotinin from the protease by chromatography on a molecular-sieve column or by filter dialysis. Aprotinin is only cleaved slowly by most proteases, if at all.

APROTININ AS API:
If interested in this product as an active pharmaceutical ingredient, please refer to the API and Intermediate page.