Trypsin from bovine pancreas
SIGMA/T9201 - powder, ≥7,500 BAEE units/mg solid
Synonym: Serine Protease 1
CAS Number: 9002-07-7
EC Number: 232-650-8
MDL Number: MFCD00082094
Product Type: Chemical
Enterokinase activates pancreatic trypsinogen to trypsin by the hydrolysis of a hexapeptide(for bovine trypsin at the Lys6 - Ile7 peptide bond) from the NH2 terminus. Bovine trypsinogen consists of a single polypeptide chain of 229 amino acids and is cross linked by six disulfide bridges. Trypsin can autocatalytically activate more trypsinogen to trypsin. Trypsin consists of a single chain polypeptide of 223 amino acid residues. This native form of trypsin is refered to as β-trypsin. Autolysis of β-trypsin (which is cleaved at Lys131- Ser132 in the bovine sequence) results in α-trypsin which is held together by disulfide bridges.
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: T9201-10G
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: T9201-5G
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: T9201-100MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: T9201-1G
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: T9201-500MG
| composition | , ≥90 % protein |
| form | powder |
| impurities | ≤3 BTEE units/mg solid Chymotrypsin |
| mol wt | 23.8 kDa |
| Quality Level | 300  |
| specific activity | ≥7,500 BAEE units/mg solid |
| storage temp. | −20°C |
| Application: | For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. |
| Biochem/physiol Actions: | Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity. Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin. |
| Caution: | Solutions in 1 mM HCl are stable for 1 year in aliquots and stored at -20°C. The presence of Ca2+ will also diminish the self-autolysis of trypsin and maintain its stability in solution. Trypsin will also retain most of its activity in 2.0 M urea, 2.0 M guanidine HCl, or 0.1% (w/v) SDS. |
| Components: | Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family. |
| Packaging: | 1, 5, 10 g in poly bottle |
| Packaging: | 100, 500 mg in poly bottle |
| Preparation Note: | This product is from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL. |
| Unit Definition: | One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate. |
| Symbol |   GHS07,GHS08 |
| Signal word | Danger |
| Hazard statements | H315 - H319 - H334 - H335 |
| Precautionary statements | P261 - P264 - P271 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 |
| Hazard Codes | Xn |
| Risk Statements | 36/37/38-42 |
| Safety Statements | 22-24-26-36/37 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| activity | specific activity: ≥7,500 BAEE units/mg solid |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.21.4 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |