Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE

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

50, 100, 250, 500 mg in glass bottle

1, 5, 100 g in glass bottle

Preparation Note

Soluble in 1 mM HCl at 1 mg/mL. It is also TPCK-treated and dialyzed. Treatment with L-1-Tosylamide-2-phenylethyl chloromethyl ketone (TPCK) reduces the chymotrypsin activity which is usually present in trypsin.

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.

No detailed specifications are available for this product.

There are no downloads for this product.

Code Description Quality Level Manufacturer Composition Storage Temp. Solubility Form Price Quantity
3581399 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
£116.72 (exc VAT) per 100MG
-
+
3581400 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
£600.32 (exc VAT) per 1G
-
+
3581401 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
£183.86 (exc VAT) per 250MG
-
+
3581402 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
£320.36 (exc VAT) per 500MG
-
+
3581403 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
£64.91 (exc VAT) per 50MG
-
+
3581404 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH - −20°C hydrochloric acid: soluble 1 mM essentially salt-free, lyophilized powder
Click Add to Quote for price and delivery
-
+
3581482 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH protein, ≥95% - hydrochloric acid: soluble 1 mM, clear essentially salt-free, lyophilized powder
£169.93 (exc VAT) per 100MG
-
+
3581483 Trypsin from bovine pancreas, TPCK Treated, essentially salt-free, lyophilized powder, >=10,000 BAEE 200 SIGMA-ALDRICH protein, ≥95% - hydrochloric acid: soluble 1 mM, clear essentially salt-free, lyophilized powder
£71.87 (exc VAT) per 50MG
-
+