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Cat. No.: RPTYP-100 (for 100mg)

Cat. No.: RPTYP-1k (for 1g)

Description

Trypsin is a serine protease that specifically cleaves peptide bonds at the C-terminal side of lysine and arginine residues. This product is produced by microbial recombinant expression and has an amino acid sequence identical to that of porcine pancreas-derived trypsin. Recombinant porcine trypsin exhibits the same enzymatic properties as animal-derived porcine trypsin and can be used as a substitute in various biotechnological processes, such as recombinant insulin production, cell culture, cell fermentation, protein hydrolysis, and cell dissociation from various tissues. Trypsin activity is inhibited by serine protease inhibitors like PMSF and by metal ion chelators like EDTA.

Product Characteristics

• Product Grade: Molecular biology grade, sterile dry powder
• CAS Number: 9002-07-7
• E.C. Number: 3.4.21.4
• Product Specifications: 100mg/vial, 500mg/vial, 1g/bottle, 5g/bottle, etc.
• Molecular Weight: Not less than 24kDa
• Purity: ≥70% β-Trypsin, ≤20% α-Trypsin
• Protein Content: ≥90%
• Enzyme Activity: >10000 U/mg lyophilized powder
• Mycoplasma: Not detected
• Endotoxin: ≤10 EU/mg
• Microorganisms: ≤5 cfu/g
• Optimal pH Range: 7-11
• Optimal Temperature Range: Recommended range is 25-37°C, with highest activity at 37°C
• Dilution Buffer: 1 mM HCl (pH3.0)
• Storage Buffer: 1 mM HCl or 50 mM Acetic Acid
• Storage Conditions: Transported at low temperature, recommended sealed storage below -20°C
• Unit Activity Definition: At 25°C, pH 7.6, in a reaction system of 3.2mL (1 cm path length), the amount of enzyme required to hydrolyze BAEE causing an increase in absorbance at 253 nm by 0.001 per minute defines one unit of trypsin activity (U).

Only for research and not intended for treatment of humans or animals

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