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| Product Name | Recombinant Trypsin (Powder) |
| Catalog No. | RESK-0249 |
| Description | Trypsin (EC 3.4.21.4) is a serine protease that specifically cleaves peptide bonds formed at the C-terminus of lysine and arginine residues. This product is expressed by recombinant Escherichia coli and purified by chromatography. Its amino acid sequence is identical to that of porcine pancreas-derived trypsin, and no animal-derived raw materials are used in the production process, eliminating exogenous viral contamination. It can replace porcine pancreas-derived trypsin in a variety of biotechnological processes, such as cell culture, cell fermentation, enzymatic digestion of proteins, and cell isolation from various tissues. The product is of high purity and free of contaminating enzymes; host cell protein and DNA residuals meet pharmacopoeia standards, avoiding the impact of impurities on cell growth. The optimal pH is 7.0-9.0, and the most stable pH is 2 +/- 0.5. |
| Intended Use | Replacement for porcine pancreas-derived trypsin in biotechnological processes including cell culture, cell fermentation, enzymatic digestion of proteins, and cell isolation from various tissues. For research use only. |
| Principle / Technology | Serine protease (EC 3.4.21.4) expressed by recombinant Escherichia coli and purified by chromatography; specifically hydrolyzes peptide bonds at the C-terminal side of lysine and arginine residues. The amino acid sequence is identical to porcine pancreatic trypsin. |
| Sample Type | Adherent cells in culture, fermentation processes, protein samples for enzymatic digestion, and various tissues for cell isolation. |
| Performance Range / Specifications | beta-Trypsin: >=70% alpha-Trypsin: <=20% Activity: >3800 USP units/mg No exogenous viral contamination; free of contaminating enzymes such as chymotrypsin Host cell protein and DNA residuals comply with pharmacopoeia standards Optimal pH: 7.0-9.0; most stable pH: 2 +/- 0.5 |
| Specificity | Specifically cleaves peptide bonds formed at the C-terminus of lysine and arginine residues; free of chymotrypsin and other contaminating enzymes. |
| Reaction Conditions / Protocol | 1. This product is a lyophilized powder; store it under the recommended conditions immediately upon receipt. 2. Before opening the cap, centrifuge at approximately 8,000-12,000 g for 10-30 seconds to collect protein adhering to the cap or tube wall at the bottom. 3. Dissolve the lyophilized powder by gentle pipetting or gentle swirling; do not shake vigorously to avoid protein denaturation and loss of activity. 4. The recommended working ratio of enzyme to target protein is 1:50 to 1:1000. Determine the optimal working concentration by consulting relevant literature or by experimental optimization for the specific purpose, cells, or animals. |
| Components / Formulation | Lyophilized recombinant trypsin powder; produced without any animal-derived raw materials. |
| Storage Conditions | Store the lyophilized powder dry at 2-8 °C. After reconstitution, store at -25 to -15 °C, avoid repeated freeze-thaw cycles, and protect from light. |
| Shelf Life | 2 years when stored as recommended. |
| Package Specifications | 10 mg 100 mg 1 g |
| Product Form | Lyophilized powder |
| Quality Control | Pharmacopoeia-grade; host cell protein and DNA residuals meet pharmacopoeia standards; free of contaminating enzymes such as chymotrypsin; no exogenous viral contamination. |
| Purity | High purity; beta-trypsin >=70%, alpha-trypsin <=20%. |
| Concentration | Reconstitution in ddH2O is recommended; the recommended stock concentration range is 30-100 mg/mL. |
| Activity / Unit Definition | >3800 USP units/mg. |
| Source / Origin | Recombinant Escherichia coli expression, purified by chromatography; amino acid sequence identical to porcine pancreatic trypsin; animal origin-free production process. |
| pH Range / Optimal pH | Optimal pH 7.0-9.0; most stable at pH 2 +/- 0.5. |
| Expiration Date / Stability | Valid for 2 years. Lyophilized powder: 2-8 °C, dry. Reconstituted solution: -25 to -15 °C, avoid repeated freeze-thaw cycles, protect from light. |
| Regulatory / Compliance | Pharmacopoeia-grade quality; host cell protein and DNA residuals comply with pharmacopoeia standards; no exogenous viral contamination. For research use only. |
| Compatibility | Suitable for cell culture, cell fermentation, enzymatic digestion of proteins, and cell isolation from various tissues; a direct replacement for porcine pancreas-derived trypsin. |
| Recommended Buffer System | Dissolve the lyophilized powder in ddH2O; recommended stock concentration 30-100 mg/mL. |
| Application Notes / Precautions | 1. Store the lyophilized powder under the recommended conditions immediately upon receipt. 2. Centrifuge at 8,000-12,000 g for 10-30 seconds before opening to collect protein at the bottom of the tube. 3. Dissolve by gentle pipetting or gentle swirling; avoid vigorous shaking to prevent protein denaturation. 4. Recommended enzyme-to-target protein ratio: 1:50-1:1000; optimize experimentally for each application. 5. Avoid repeated freeze-thaw cycles after reconstitution and protect from light. |
| Recognition Site | Cleaves peptide bonds at the C-terminal side of lysine and arginine residues. |
For research use only, not for clinical use.
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