Recombinant Trypsin | Introduction | Recombinant trypsin can be used for the production of recombinant insulin, the use of recombinant human proinsulin expression is imitating the natural way to synthesize insulin, mainly divided into the construction of genetically engineered bacteria and the later use of trypsin and carboxypeptidase B for enzyme digestion, trypsin is a serine protease that specifically cleaves, and the C- chain in proinsulin is cleaved off in the process. |
| Product Advantage |
Free of animal origin: recombinant production, no exogenous virus contamination, the production process does not use any animal source raw materials. Quality: Mass production can ensure stable and continuous batch production; there is no difference between product batches and the quality is stable. Purity: specific activity is high; the host protein residue is less than the limit requirement of biological products. Freeze dried powder: easy to store and transport. Compliance with regulatory requirements: The production equipment and production environment comply with relevant regulatory requirements, and the production process is fully followed. NSF ISO 9001: 2015 quality system and comply GMP guiding principles. Quality documents complete: According to customer needs, can provide relevant regulatory support documents. |
| Enzymatic Properties | Recombinant porcine trypsin has the same enzymatic properties as animal-derived porcine trypsin and can be used in various biotechnological processes instead of porcine pancreatic trypsin. |
| Basic Characteristics | Molecular weight of recombinant trypsin 24kD, the most suitable pH7.0-11.0. Activity by serine protease inhibitors such PMSF, etc., metal ion chelating agents suchEDTA, etc. |
| Method of Use | The amount of enzyme: target protein= 1: 50-1: 1000, the most suitable pH7.0-11.0. |
| Product Use |
Cell culture aspects 1. Acquisition of primary cells for digestion and dissociation of tissue blocks 2. For passage digestion of adherent cells 3. Digestion of cells for microcarrier method culture 4. Used to prohibit contact with animal sources of biopharmaceuticals and other fields Molecular Field 1. For specific protein enzymatic hydrolysis 2. Protein sequencing, proteomics research 3. Making peptide map 4. and PAGE gels |
| Sizes | 10mg; 100mg; 1g |
| Cutting Sites | Trypsin is a serine protease that specifically cleavesamino acid (Lysine, K) and arginine (Arginine, R) Cterminal peptide bonds. |
| Amino Acid Sequence | Recombinant porcine trypsin was expressed and produced by recombinant E. Coli, and the amino acid sequence was completely consistent with that of porcine pancreatic trypsin. |
| Appearance | White or off-white crystalline powder |
| Specific Activity | ≥ 3800 USP units/mg pro. |
| Molecular Weight (Protein Electrophoresis) | 24.0±2.4 kDa |
| Remarks | 25°C, pH 7.6, reaction system 3.2ml (1 cmoptical path), enzymatic hydrolysis per minute BAEE make 253nm 0.003 is defined as a USP units. |
| Storage | Storage stability: recombinant trypsin freeze-dried powder stored in 2-8°C, 24 months of stability; 1 mM HCL or 50 mM acetic acid and store it in -20°C, repeated freezing and thawing 10 times, no loss of activity. |
| Transportation | Transport stability: blue ice insulation transport, stable activity. |
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