Recombinant Porcine Trypsin

Porcine Trypsin
Recombinant, Molecular Biology Grade
From yeast cells with cloned gene encoding genetically engineered Trypsin from porcine pancreas
Catalog Number: GPE010001
CAS No.:9002-07-7E.C.: 3.4.21.4
Properties
Molecular mass>24kD
pI10.5
pH range7.0-11.0
optimum pH: 8.0
Storage Temperature-20 °C Recommended
Form White or off-white lyophilized powder
Temperature profileOptimal  37°C
Specific activity>10,000 UPS Unit/mg
Unit Definition:
One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0 mL at pH7.6 and 25℃, with BAEE as a substrate.
Purity and Quality
Purity: ≥ 90%
Protein composition: ≥70% β-trypsin, ≤ 20% α-trypsin
Product Description
General Description:
Porcine Trypsin is a serine protease that specifically cleaves peptide bonds at the C-terminal of lysine and arginine residues. This product is produced through yeast gene recombinant expression, ensuring a complete amino acid sequence identical to porcine pancreatic trypsin. Recombinant Porcine Trypsin shares enzymatic properties identical to its animal-sourced counterpart.  

Advantages:
High Purity: The recombinant form offers higher purity compared to the native enzyme, with fewer contaminating proteases and other unwanted components.
Batch Consistency: Recombinant production ensures consistent enzyme activity across different batches, which is critical for reproducibility in research and manufacturing.
Reduced Risk of Contaminants: The risk of contamination with animal-derived pathogens, such as prions or viruses, is significantly reduced in the recombinant version.
Ethical Considerations: Recombinant production avoids the ethical concerns associated with harvesting trypsin from animal sources, making it a more acceptable choice for certain users.  

Applications:
Protein Digestion:
Proteomics: Recombinant Porcine Trypsin is widely used in proteomics for digesting proteins into peptides, which are then analyzed by mass spectrometry (MS). Its ability to cleave peptides at the carboxyl side of lysine and arginine residues is critical for generating consistent and predictable peptide fragments.  
Cell Culture:
Cell Detachment: It is commonly used in cell culture to detach adherent cells from the surface of culture vessels. The recombinant form ensures minimal contamination and consistent performance, making it ideal for sensitive applications.
Biopharmaceutical Production:
Bioprocessing: In the production of biologics, such as therapeutic proteins, recombinant Porcine Trypsin is used in downstream processing to remove fusion tags from recombinant proteins or to activate precursor proteins.
Vaccine Production:
Virus Activation: It is used in the production of vaccines, especially in the activation of certain viruses during the manufacturing process.  
Food Industry:
Protein Hydrolysis: In the food industry, it can be used for the hydrolysis of proteins in the production of protein hydrolysates, which are used as flavor enhancers or nutritional supplements.
Preparation Notes
Storage buffer: 1 mM hydrochloric acid or 50 mM acetic acid
Dilution Buffer: 1 mM hydrochloric acid (pH 3.0)
Preparation Instructions
Inhibition: The activity of Porcine Trypsin is susceptible to inhibition by serine protease inhibitors such as PMSF, and metal ion chelators like EDTA can also modulate its enzymatic activity.
Stability
One year from the date of manufacture stored at 2-8℃.
Precautions and Disclaimer
This product is for R&D use only, not for drug, household, or other uses.
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