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Trypsin from bovine pancreas

TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

biological source

bovine pancreas

Quality Level


aseptically filled


essentially salt-free, lyophilized powder

specific activity

≥10,000 BAEE units/mg protein

mol wt

23.8 kDa


protein, ≥95%


hydrochloric acid: soluble 1 mM, clear

foreign activity

Chymotrypsin ≤0.1 BTEE units/mg protein

storage temp.


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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.


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.
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. Trypsin has also been used in a study to investigate BN-PAGE analysis of Trichoderma harzianum secretome.


50, 100 mg

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.

Unit Definition

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path).
One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.

Preparation Note

TPCK treated

Analysis Note

Protein determined by E1%/280

Other Notes

View more information on trypsin at


Exclamation markHealth hazard

Signal Word


Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids



Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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