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T1426

Trypsin from bovine pancreas

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

Synonym(s):

Serine Protease 1

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50 mg

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$74.10
100 mg

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$106.00
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$186.00
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About This Item

CAS Number:
9002-07-7
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-650-8
MDL number:
MFCD00082094
EC Number:
3.4.21.4 (BRENDA, IUBMB)
Specific activity:
≥10,000 BAEE units/mg protein
Biological source:
bovine pancreas

$74.10

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biological source

bovine pancreas

Quality Segment

grade

Proteomics Grade

form

essentially salt-free, lyophilized powder

specific activity

≥10,000 BAEE units/mg protein

mol wt

23.8 kDa

technique(s)

protein mass spectrometry: suitable

solubility

hydrochloric acid: soluble 1 mM

application(s)

diagnostic assay manufacturing

foreign activity

Chymotrypsin ≤0.1 BTEE units/mg protein

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.

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.

Other Notes

One BAEE unit will produce a A253 of 0.001 per minute at pH 7.6 at 25°C using BAEE as a substrate.
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.

Disclaimer

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.

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This Item
T1005T8003T9201
Trypsin from bovine pancreas TPCK Treated, essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein

Sigma-Aldrich

T1426

Trypsin from bovine pancreas

Trypsin from bovine pancreas Type XI, lyophilized powder, ≥6,000 BAEE units/mg protein

Sigma-Aldrich

T1005

Trypsin from bovine pancreas

Trypsin from bovine pancreas Type I, ~10,000 BAEE units/mg protein

Sigma-Aldrich

T8003

Trypsin from bovine pancreas

Trypsin from bovine pancreas powder, ≥7,500 BAEE units/mg solid

Sigma-Aldrich

T9201

Trypsin from bovine pancreas

description

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

description

Type XI, lyophilized powder, ≥6,000 BAEE units/mg protein

description

Type I, ~10,000 BAEE units/mg protein

description

powder, ≥7,500 BAEE units/mg solid

biological source

bovine pancreas

biological source

bovine pancreas

biological source

-

biological source

-

technique(s)

protein mass spectrometry: suitable

technique(s)

-

technique(s)

-

technique(s)

-

specific activity

≥10,000 BAEE units/mg protein

specific activity

≥6,000 BAEE units/mg protein

specific activity

~10,000 BAEE units/mg protein

specific activity

≥7,500 BAEE units/mg solid

grade

Proteomics Grade

grade

-

grade

-

grade

-

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

solid

form

powder

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

application(s)

-

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Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class

11 - Combustible Solids

WGK

WGK 1

PPE (personal protective equipment)

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Questions

1–8 of 8 Questions  

  1. For your trypsin (e.g., T1426), what validated thermal inactivation conditions do you recommend, and can complete inactivation be achieved with ≤70 °C heating (to minimize sample protein denaturation) instead of the typical 80–95 °C for 5–10 min?

    1 answer

    1. Thermal inactivation conditions for trypsin have not been internally validated. As reported in the product datasheet, trypsin is reversibly denatured at high pH (above 11), by precipitation with TCA, or by high concentrations of urea (greater than 6.5 M) and irreversibly denatured by heating at 100 °C in 1% (w/v) SDS for 5 minutes is required.

      Please see the link below to review additional information available in the product datasheet:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/136/179/t1426pis-ms.pdf

      The following publication may also be of interest:
      https://pmc.ncbi.nlm.nih.gov/articles/PMC2728467/

      Helpful?

  2. Hello, we need for our experiments purified cationic trypsin. Did you ever confirm that the bovine trypsin you sell is cationic trypsin or PRSS1. Thanks

    1 answer

    1. This product is the native form of trypsin, beta-trypsin. This product had not been cofirmed to be cationic nor anionic isoform.

      Helpful?

  3. I would like to ask, is the Trypsin, TPCK-treated already sterile when I solve the powder in sterile aquadest, or have I to filter the solution?

    1 answer

    1. This product is not sterile and will need to be sterile filtered. See product SLGP33RS, Millex GP, for a suitable filter options:
      https://www.sigmaaldrich.com/product/mm/slgpr33rs

      Helpful?

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

    1 answer

    1. 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.

      Helpful?

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

    1 answer

    1. 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.

      Helpful?

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

    1 answer

    1. 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.

      Helpful?

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

    1 answer

    1. 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.

      Helpful?

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

    1 answer

    1. 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.

      Helpful?

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