Trypsin, Mass Spec Grade
The product is for non-human research only. Not for therapeutic or veterinary use.
Catalog Number: BT-224144
Molecular Weight: 23kDa
Formulation: Mass spectrometry modified trypsin is supplied by lyophilized powder.
|Product Name||Trypsin, Mass Spec Grade|
|Formulation||Mass spectrometry modified trypsin is supplied by lyophilized powder.|
|Description||Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC peptide analysis. In addition, auto- proteolysis can result in the generation of pseudo trypsin, which has been shown to exhibit chymotrypsin-like specificity. Our Scientific Mass Spec Grade Modified Trypsin is porcine trypsin modified by reductive methylation, rendering it resistant to proteolysis digestion . In enzymatic stability tests, modified trypsin was not found to self-hydrolysis and retain higher the activity of general trypsin.|
|Product Background||Trypsin (EC 188.8.131.52) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins. Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin was discovered in 1876 by Wilhelm Kühne.In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream. Tryptic digestion is a necessary step in protein absorption, as proteins are generally too large to be absorbed through the lining of the small intestine.|
|Reconstitution||Trypsin Resuspension Buffer is composed of 1mM hydrochloric acid|
|Stability||Trypsin are stable for up to 2 years from date of receipt at -20℃. Modified trypsin is maximally active in the pH range of 7–9 and reversibly inactivated at pH 4.|
|Storage||Store the lyophilized Trypsin powder at –20°C. Store reconstituted enzyme at –70°C.|
|Usage||For maximum activity, resuspend Mass Spectrum Grade Modified Trypsin in the Trypsin Resuspension Buffer provided, and heat at 30°C for 15 minutes before use..-Thaw the reconstituted trypsin at room temperature, placing on ice immediately after thawing. Remove the amount of trypsin needed, then refreeze the unused portion at -70℃. To maintain maximum product activity, limit the number of freeze-thaw cycles to five or dispense into single-use aliquots after resuspending.A protease protein ratio of 1 100 to 1 25(w/w) is recommended for protein identification or PTM for 13-16 hours at 37°C|
|Last Modified||Aug 20 2021|