Analytical Data
-
Gene name
Trypsin
- Application
-
Species
Pig
-
Source
Yeast
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P00761
-
Expression Region
Phe1~Asn231
-
Molecular Weight
27kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Trypsin is a serine protease that plays a crucial role in the digestive system by breaking down proteins into smaller peptides in the small intestine. Its activity is essential for nutrient absorption and protein metabolism, making it a significant enzyme not only in physiological processes but also in various industrial applications such as food processing, pharmaceuticals, and biotechnology. The recombinant production of trypsin through molecular biology techniques has gained attention as it allows for the generation of a more consistent and high-yielding enzyme source compared to traditional extraction methods from animal tissues. This approach also enables the modification of trypsin to enhance its stability, specificity, and activity under various conditions. Additionally, recombinant trypsin can facilitate studies related to protein structure and function, as well as serve as a vital tool in proteomics research. As the demand for highly pure and active enzymes continues to rise, ongoing research focuses on optimizing expression systems, improving yield, and characterizing the properties of recombinant trypsin to meet industrial and scientific needs. This has implications for not only enzyme applications but also advances in therapeutic developments, highlighting the importance of trypsin in both basic and applied research contexts.
