Trypsin Bovine
Greater than 90% as determined by SDS-PAGE.
Description
Recombinant Bovine Trypsin is free from any animal and human sources. Trypsin Bovine specifically cleaves peptide bonds after basic amino acids such as lysine and arginine.
Product Specs
Trypsin, a serine protease present in the digestive systems of many vertebrates, plays a crucial role in protein digestion. Produced in the pancreas as the inactive proenzyme trypsinogen, trypsin becomes activated in the duodenum. Its primary function is to break down proteins into smaller peptides by cleaving peptide bonds specifically after lysine and arginine amino acids, except when followed by proline. This enzymatic activity is essential for efficient protein absorption in the ileum. Trypsin functions optimally at a pH of approximately 8 and a temperature of around 37°C. A deficiency in trypsin and other digestive enzymes' transport from the pancreas is linked to cystic fibrosis. Due to its abundance in the pancreas and ease of purification, trypsin finds widespread use in various biotechnological applications.
Recombinant Bovine Trypsin is characterized by its production without using any animal-derived or human-derived materials. This enzyme specifically cleaves peptide bonds following the basic amino acids lysine and arginine.
To reconstitute the lyophilized Bovine Trypsin, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. Once reconstituted, it can be further diluted in other aqueous solutions as needed.
To ensure optimal stability, store the Bovine Trypsin at a temperature between 2-8°C. Avoid freezing.
Purity level exceeding 90% as determined by SDS-PAGE analysis.
The biological activity is determined to be 4,313 Units per mg.
Product Science Overview
Bovine trypsin is traditionally extracted from the pancreas of cattle. However, due to concerns about contamination with infectious agents and the increasing demand for high-quality trypsin, recombinant techniques have been developed. Recombinant trypsin is produced by inserting the gene encoding trypsin into a suitable host organism, such as the yeast Pichia pastoris . This method ensures a consistent and high-quality product that is free from animal-derived contaminants.
The structure of bovine trypsin was first elucidated in the 1970s . It consists of a single polypeptide chain with a molecular weight of approximately 24 kDa. The enzyme’s active site contains a catalytic triad composed of histidine, aspartate, and serine, which is essential for its proteolytic activity.
Recombinant bovine trypsin retains the same structural and functional characteristics as its native counterpart. It exhibits high specificity for cleaving peptide bonds at lysine and arginine residues, making it an invaluable tool in various biotechnological and pharmaceutical applications.
Recombinant bovine trypsin is widely used in the biopharmaceutical industry for several purposes:
- Protein Digestion: It is used to digest proteins into smaller peptides for mass spectrometry analysis.
- Cell Culture: Trypsin is employed to detach adherent cells from culture vessels during cell passaging.
- Insulin Production: It plays a critical role in the conversion of proinsulin to insulin during the manufacturing process .
The recombinant production of bovine trypsin offers several advantages over traditional extraction methods:
- Purity: Recombinant trypsin is free from animal-derived contaminants, reducing the risk of introducing pathogens.
- Consistency: The production process is highly controlled, ensuring a consistent and high-quality product.
- Scalability: Recombinant techniques allow for large-scale production to meet the increasing demand for trypsin in various industries.
In conclusion, recombinant bovine trypsin is a vital enzyme with numerous applications in biotechnology and pharmaceuticals. Its production through recombinant techniques ensures a high-quality, consistent, and safe product that meets the stringent requirements of modern biopharmaceutical manufacturing.
