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T9201

Sigma-Aldrich

Trypsin from bovine pancreas

powder, ≥7,500 BAEE units/mg solid

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Synonym(s):
Serine Protease 1
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

powder

specific activity

≥7,500 BAEE units/mg solid

mol wt

23.8 kDa

composition

, ≥90 % protein

impurities

≤3 BTEE units/mg solid Chymotrypsin

storage temp.

−20°C

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This Item
T1005T7309T9935
vibrant-m

T9201

Trypsin from bovine pancreas

vibrant-m

T1005

Trypsin from bovine pancreas

vibrant-m

T7309

Trypsin from bovine pancreas

vibrant-m

T9935

Trypsin from bovine pancreas

mol wt

23.8 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

mol wt

23.8 kDa

form

powder

form

lyophilized powder

form

solid

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

200

impurities

≤3 BTEE units/mg solid Chymotrypsin

impurities

salt, essentially free

impurities

-

impurities

-

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.

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.

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.

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

This product is from pancreas sourced from New Zealand. It is soluble in 1 mM HCl at 1 mg/mL.

replaced by

pictograms

Exclamation markHealth hazard

signalword

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_germany

WGK 1

ppe

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


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Wahyu Wijaya et al.
Current research in food science, 2, 11-19 (2020-09-12)
In this work, the bioaccessibility of polymethoxyflavones (PMFs) loaded in high internal phase emulsions (HIPE, ϕoil = 0.82) stabilized by whey protein isolate (WPI)-low methoxy pectin (LMP) complexes was evaluated using in vitro lipolysis and dynamic in vitro intestinal digestion studies. PMFs
Rasmus Karstad et al.
Journal of medicinal chemistry, 55(14), 6294-6305 (2012-06-23)
This study investigates how the S1 and S3 site of trypsin can be challenged with cationic amino acid analogues to yield active antimicrobial peptides with stability toward tryptic degradation. It is shown that unnatural analogues can be incorporated to generate
David von Stetten et al.
Journal of synchrotron radiation, 27(Pt 3), 844-851 (2020-05-10)
ID30A-3 (or MASSIF-3) is a mini-focus (beam size 18 µm × 14 µm) highly intense (2.0 × 1013 photons s-1), fixed-energy (12.81 keV) beamline for macromolecular crystallography (MX) experiments at the European Synchrotron Radiation Facility (ESRF). MASSIF-3 is one of two fixed-energy beamlines sited on
Vandana Shashi et al.
Human mutation, 40(8), 1115-1126 (2019-07-03)
Encoding the slow skeletal muscle isoform of myosin binding protein-C, MYBPC1 is associated with autosomal dominant and recessive forms of arthrogryposis. The authors describe a novel association for MYBPC1 in four patients from three independent families with skeletal muscle weakness
Claire E J Waterborg et al.
PloS one, 13(10), e0205902-e0205902 (2018-10-20)
Rheumatoid arthritis is an auto-immune disease of the synovial joints, hallmarked by chronic inflammation and subsequent progressive tissue destruction. TYRO3, AXL and MER (gene name Mertk) (TAM) receptors are part of a negative feedback signaling system in the immune reaction

Protocols

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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