Cat. No.:
CSI14646B
pdf (datasheet)
Description:
Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyzes peptide bonds in which the carbonyl group is contributed by the basic amino acids lysine or arginine. Trypsin is produced in the pancreas as the inactive proenzyme, Trypsinogen, which is converted to the active trypsin by enterokinase from the intestinal mucosa and by trypsin itself.. Trypsin is one of the three principal digestive proteinases, the other two being Pepsin and Chymotrypsin. The optimum pH for trypsin is in the range of 7-9. Calcium ions contribute to increasing the stability of trypsin, while several protein-like substances inhibit the activity of trypsin. These trypsin inhibitors have been isolated from soybean, barley, mung bean and pancreas.
Molecular Weight:
23.5 kDa
Physical State:
Lyophilized
Biological Activity:
One unit is the amount of enzyme which causes an increase in absorbance of 0.003 per minute at 25ºC and 253 nm, pH 7.6, on the substrate benzoyl-L-arginine ethyl ester (BAEE)
Specific Activity:
~5,000 U/mg, lot specific
Reconstitution:
Soluble in distilled water or dilute buffer
Storage/Stability:
Store at -20°C for up to 1 year.
