Aprotinin, Active, Bovine recombinant protein (AOF)
BPTI, Basic protease inhibitor, Pancreatic trypsin inhibitor
|Calculated MW||9.7 kDa (36-93 aa + N-terminal Poly-his tag)|
|Other Names||BPTI, Basic protease inhibitor, Pancreatic trypsin inhibitor|
|Assay&Purity||SDS-PAGE ; ≥90%|
|Application Notes||Centrifuge the vial prior to opening at low speed. Reconstitute in water to a concentration of 1 mg/ml. The solution can then be diluted into PBS or other aqueous buffers and store at 4°C for 1 week or –20°C for future use. For long-term storage, it is recommended to add a carrier protein (e.g., 0.1% BSA). Avoid repeated freezing and thawing cycles.|
|Storage||-20°C; Lyophilized from 5 mg/ml solution in PBS|
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Provided below are standard protocols that you may find useful for product applications.
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. It is present in blood and in most tissues, with a high concentration in lung, inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, Aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins. Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids arranged in a single polypeptide chain, cross-linked by three disulfide bridges. BioVision’s Recombinant Bovine Aprotinin is an animal-origin free protein purified by proprietary chromatographic techniques.
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Creighton T.E.,et al.Cold Spring Harb. Symp. Quant. Biol. 52:511-519(1987).
Kingston I.B.,et al.Biochem. J. 233:443-450(1986).
Anderson S.,et al.Proc. Natl. Acad. Sci. U.S.A. 80:6838-6842(1983).
Kassell B.,et al.Biochem. Biophys. Res. Commun. 20:463-468(1965).
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