TRYPZEAN(TM) Chemical Properties

storage temp. 

2-8°C

form 

lyophilized powder

biological source

bovine pancreas (trypsin)

Specific Activity

≥8,500BAEE units/mg protein (biuret)

Safety Information

Hazard Codes 

Xn,Xi

Risk Statements 

36/37/38-42/43-42

Safety Statements 

23-45-36/37-26-24-22

WGK Germany 

3

RTECS 

YN5075000

F 

1-3-10

MSDS

• Language:English Provider:SigmaAldrich

TRYPZEAN(TM) Usage And Synthesis

Uses

Trypsin has been used in a study to assess the ontogeny of the endocrine pancreas in the fetal/newborn baboon. Trypsin digestion and hydrogen/deuterium exchange support the transition between inward- and outward-facing conformations during the catalytic cycle of the bacterial multidrug ATP-binding cassette transporter.

Uses

A very active and very stable trypsin agarose derivative has been used to optimize the design of the synthesis of a model dipeptide, benzoylarginine leucinamide. Trypsin has also been used in a study to investigate protonation-state determination in proteins using high-resolution X-ray crystallography.

General Description

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

Biochem/physiol Actions

Lys-acetylated trypsin is less susceptible to autolysis than the native form.

Description

Recombinant Bovine Trypsin is free from any animal and human sources. Trypsin Bovine specifically cleaves peptide bonds after basic amino acids such as lysine and arginine.

Source

Corn

Background

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°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.

TRYPZEAN(TM)()Related Product Information

• TPCK