protein

Recombinant Bovine Trypsin

MBS142869

1 mg

140 USD

Recombinant Protein

Recombinant Bovine Trypsin

BTrypsin

Trypsin Bovine; Trypsin Bovine Recombinant; bTrypsin

Corn

Greater than 90% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

The protein was lyophilized without any additives. Sterile Filtered lyophilized powder.

Bovine Trypsin although stable at room temp for 1 week, should be stored desiccated below -18 degree C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Solubility: It is recommended to reconstitute the lyophilized Bovine Trypsin in sterile 18M Omega -cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions. Biological Activity: 3,650 Units/mg.

RECOMBINANT & NATURAL PROTEINS; Recombinant Proteins; Trypsin

Description: Recombinant Bovine Trypsin is free from any animal and human sources.% of inhibition is equal to bovine trypsin. Introduction: Trypsin is a serine protease that hydrolyses proteins, it is found in the digestive system of numerous vertebrates. Trypsin is produced as the inactive proenzyme trypsinogen in the pancreas. Trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin is secreted into the duodenum, where it acts to hydrolyses peptides into amino acids, which is necessary for the uptake of protein in the food even though peptides are smaller than proteins; they are still too big to be absorbed through the lining of the ileum. The optimal operating pH for Trypsins is about 8 and about 37 degree C temperature. In cystic fibrosis disease there is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. Trypsin is widely used in various biotechnological processes since it's available in high quantity in the pancreases, and can be purified rather easily.

1 mg

140 USD

10 mg

205

100 mg

745