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:

Quality Level


essentially salt-free, lyophilized powder

specific activity

≥10,000 BAEE units/mg protein

mol wt

23.8 kDa


hydrochloric acid: soluble 1 mM

Featured Industry

Diagnostic Assay Manufacturing

foreign activity

Chymotrypsin ≤0.1 BTEE units/mg protein

storage temp.


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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.


50, 100, 250, 500 mg in glass bottle
1, 5, 100 g in glass bottle

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.


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.


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.

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.

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.


Exclamation markHealth hazard

Signal Word


Hazard Statements

Target Organs

Respiratory system

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Certificate of Analysis

Certificate of Origin

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. What is Product T1426, Trypsin from bovine pancreas, soluble in, and how do you recommend storing solutions?

    Trypsin is soluble in 1 mM hydrochloric acid (pH approximately 3). It is also surprisingly stable in 1 mM HCl. Solutions are stable for approximately 1 year when aliquoted and stored at -20°C. The presence of Ca2+ (20 mM) will also retard trypsin's ability to autodigest, and will therefore help to maintain the stability of the trypsin in solution.

  4. How much of Product T1426, Trypsin from bovine pancreas, should I use to digest my peptide?

    For trypsin digestion of peptides, use a ratio (w:w) of about 1:100 to 1:20 for trypsin:peptide. Trypsin preparations usually contain some contaminating chymotrypsin and this should be inhibited with N-tosyl-L-phenylalanyl chloromethyl ketone (TPCK). Product No. T1426 has already been treated with TPCK, so it does not need to be further treated.

  5. What is the extinction coefficient for Product T1426, Trypsin from bovine pancreas?

    Various values have been reported in the literature for the extinction coefficient of bovine pancreatic trypsin. The E1%(280) values have ranged from 12.9 - 15.4. When we assay the protein content of Product No. T1426 in our labs here at Sigma, we use a value of 14.4.

  6. Does Product T1426, Trypsin from bovine pancreas, work for in-gel digestions?

    For in-gel digestions, we actually recommend using a methylated trypsin. Product No. T6567 is Trypsin from porcine pancreas, proteomics grade, dimethylated. For product T6567, the lysine residues of proteomics grade trypsin have been reductively methylated, resulting in a product that is resistant to autolysis. The T6567 has also been treated with TPCK to remove chymotryptic activity, further purified through affinity chromatography, and lyophilized. This results in an enzyme that gives highly specific cleavage.

  7. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  8. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

  10. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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Molecular & cellular proteomics : MCP, 10(4), M110-M110 (2011-01-20)
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PolyGly is present in many proteins in various organisms. One example is found in a transmembrane β-barrel protein, translocon at the outer-envelope-membrane of chloroplasts 75 (Toc75). Toc75 requires its N-terminal extension (t75) for proper localization. t75 comprises signals for chloroplast...
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Highly pathogenic influenza A viruses (IAV) from avian hosts were first reported to directly infect humans 20 years ago. However, such infections are rare events, and our understanding of factors promoting or restricting zoonotic transmission is still limited. One accessory...
This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).
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