Trypsin-2 Human
Description
Recombinant Human Trypsin-2 expressed in E.Coli having an Mw of 24kDa is purified by standard chromatography techniques.
Product Specs
Recombinant Human Trypsin-2, with a molecular weight of 24 kDa, is expressed in E. coli and purified using standard chromatography techniques.
The protein was lyophilized without the addition of any other substances.
It is recommended to reconstitute the lyophilized Human Trypsin in sterile 1mM HCl or 50mM HAC at a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions.
Recombinant Human Trypsin is stable at room temperature for 1 week but should be stored in a dry environment below -18°C. For long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
One USP unit of trypsin activity is defined as the amount of enzyme that catalyzes a change in absorbance at 253 nm (ΔA253) of 0.003 per minute in a 3.0 ml reaction volume at pH 7.6 and 25°C, using BAEE as the substrate (1 cm light path).
The biological activity is 2,800 units per mg of protein.
For trypsin digestion, a weight ratio of 1:50 to 1:1000 (enzyme:substrate) is recommended.
Product Science Overview
Trypsin-2 is synthesized in the pancreas as an inactive precursor called trypsinogen-2 . This zymogen is secreted into the duodenal lumen, where it is activated by the enzyme enteropeptidase . The activation process involves the cleavage of a specific peptide bond in trypsinogen-2, resulting in the formation of active trypsin-2 . Once activated, trypsin-2 can further activate other digestive enzymes, including additional trypsinogen molecules, chymotrypsinogen, and procarboxypeptidases .
In the digestive system, trypsin-2 is essential for the efficient breakdown of dietary proteins . It cleaves peptide bonds at the carboxyl side of lysine and arginine residues, producing smaller peptides that can be further degraded by other proteases . This process is vital for the absorption of amino acids and peptides in the small intestine.
Recombinant human trypsin-2 is produced using genetic engineering techniques, where the PRSS2 gene is inserted into a suitable expression system, such as a mouse myeloma cell line . The recombinant enzyme is then purified to high levels of purity, typically greater than 95%, and is free from endotoxins . This recombinant form is used in various research and industrial applications, including protein digestion, cell culture, and the activation of other enzymes .
Trypsin-2 has been implicated in several pancreatic diseases and conditions . In cases of chronic pancreatitis and pancreatic cancer, the levels of trypsin-2 are often elevated . Additionally, trypsin-2 is up-regulated in individuals with chronic alcoholism . These associations make trypsin-2 a potential biomarker for the diagnosis and monitoring of pancreatic disorders.
