Sigma-Aldrich Trypsin from porcine pancreas

Sigma-Aldrich Trypsin from porcine pancreas is a highly active, native serine protease widely used in protein digestion, cell culture, and biochemical research. This enzyme cleaves peptide bonds C-terminal to lysine and arginine residues, making it ideal for peptide mapping, mass spectrometry sample prep, and protein structure-function studies.

This product is supplied as a lyophilized powder and is soluble in Hank's Balanced Salt Solution (HBSS) at 25 mg/mL. It is commonly used for cell dissociation, tissue disaggregation, and in-gel protein digestion in proteomics workflows.

Key Features and Benefits

• Broad utility in proteomics, cell biology, and peptide digestion
• Cleaves at lysine and arginine residues unless followed by proline
• Maintains activity in 2 M urea, guanidine HCl, or 0.1% SDS
• EDTA-compatible for use in calcium/magnesium-free buffers
• Inhibited by serine protease inhibitors (e.g., TLCK, APMSF, aprotinin)
• Soluble in 1 mM HCl; solutions stable at –20 °C for 1 year in aliquots
• Available in pack sizes ranging from 5 g to 500 g

Biochem/Physiological Actions

• Catalyzes peptide bond hydrolysis C-terminal to Arg and Lys
• Inhibited by acidic residues and blocked if Pro is adjacent
• Optimal activity at pH 7–9
• Retains activity in various denaturants
• Requires Ca²⁺ to prevent autolysis; EDTA removes divalent cations to enhance activity

Component Information

• Single-chain polypeptide of 223 amino acids
• Derived from trypsinogen via cleavage at Lys–Ile
• Cross-linked by six disulfide bridges
• Yields β-trypsin; autolysis forms α-trypsin

Unit Definition

One BAEE unit hydrolyzes Nα-Benzoyl-L-arginine ethyl ester (BAEE) to produce a ΔA253 of 0.001 per minute at pH 7.6 and 25 °C.

Note: 1 BTEE unit = 320 ATEE units.

Preparation Notes

• Soluble in HBSS (25 mg/mL)
• Use EDTA-containing buffers for cell culture applications
• Avoid Ca²⁺ and Mg²⁺ for enhanced proteolytic activity in digestion protocols

Available Pack Sizes

Applications

• Proteomics: in-gel digestion, peptide mapping, mass spectrometry sample prep
• Cell culture: dissociation of adherent cells and tissue disaggregation
• Biochemical research: protein cleavage, crystallization studies, folding analysis
• Structural biology: studying protein kinetics, yield, and conformational changes

Sigma-Aldrich Trypsin from Porcine Pancreas offers a reliable and well-characterized solution for protein digestion, enzymology, and cell culture. With high specificity, broad application, and multiple pack sizes, it is a trusted reagent across research, industrial, and academic laboratories.