Source: Recombinant bovine aprotinin, genetically engineered E.coli production
Storage temperature: -20℃ and below, away from light storage
Protein sequence: Amino acid sequence is identical with aprotinin derived from bovine lung
一、Product introduction
Aprotinin is a competitive inhibitor of serine protease, which can inhibit the activities of trypsin, chymotrypsin and kininogenase. Aprotinin can form stable complexes with proteases to block the active site of the enzyme. Most aprotin-protease complexes unbind at pH <3. Aprotinin can be isomolar bound to proteases. Recombinant aprotinin of this product is expressed by recombinant Escherichia coli and purified by multiple columns. The recombinant aprotinin has the same enzymatic properties as animal-derived aprotinin, and can replace animal-derived aprotinin and serum for the neutralization of trypsin and other serinases, and can be used in the biological process of cell culture and oral administration of protein.
二、Product characteristics
| Source | Recombinant E. coli |
| Appearance | Clear, colorless to light yellow liquid |
| Specific activity | ≥3.0EPU/mg pro. |
| Absorbance(277nm) | ≤0.8(3EPU/ml aqueous solution) |
| Purity(SDS-PAGE) | ≥95% |
This product enzyme activity unit: can inhibit the activity of a trypsin unit called an aprotinin activity unit (EPU).
Trypsin unit: 1μmol of N-benzoyl-L-arginine ethyl ester (BAEE) can be hydrolyzed into one trypsin unit (microkatal) per second.
三、Usage method
Aprotinin and protease are equimolar effective binding, the recommended binding pH >6.0, and do not bind under pH <3.0 conditions.
Application case: In the process of protein digestion, adding the ratio of aprotinin to recombinant trypsin between 4:5 and 8:5 can completely inhibit the further digestion of trypsin, and the specific cell culture inhibition reaction needs to be adjusted according to the actual situation of the cell digestive fluid.
四、Storage and stability
Enzyme liquid storage stability: Recombinant aprotinin liquid storage at -20℃, stable for 24 months. Repeated freezing and thawing, no significant loss of activity.
Transport stability: blue ice insulation transport, stable activity.
五、Product advantage
No animal origin: Reconstituted production, no exogenous virus pollution, the production process does not use any animal source raw materials.
Stable quality: mass production (10+g grade production and supply), to ensure stable and continuous batch production; There is no difference between batches and the quality is stable.
High purity: The host protein residue is less than the biological product limit requirements.
Compliance with regulatory requirements: The production equipment and production environment meet the relevant regulatory requirements, and the production process fully complies with the NSF ISO 9001:2015 quality system and to a certain extent complies with the guiding principles of GMP for the production of raw materials.
Complete quality documents: According to customer needs, relevant regulatory support documents can be provided.
六、Product use
Aprotinin is a competitive inhibitor of serine protease, which can inhibit the activities of trypsin, chymotrypsin and kininogenase.
Aprotinin can form stable complexes with proteases to block the active site of the enzyme. Recombinant aprotinase has the same enzymatic properties as animal-derived aprotinase, and can replace animal-derived aprotinase in various biotechnological processes, such as: inhibiting serine protease activity in recombinant protein production; Cell culture, etc.