![Recombinant Porcine Trypsin](https://user-images.strikinglycdn.com/res/hrscywv4p/image/upload/c_limit,fl_lossy,h_1000,w_500,f_auto,q_auto/2311560/327637_508188.png)
Recombinant Porcine Trypsin
$125.00 - $845.00
All products have special prices for bulk purchase, please contact for more details if required.
Cat. No.: PTYP-10 (for 10mg)
Cat. No.: PTYP-100 (for 100mg)
Description
Pancreatic trypsin is a serine protease that specifically cleaves peptide bonds at the carboxyl end of arginine and lysine. Recombinant porcine trypsin from BiyunTian is produced by expression in Escherichia coli, and its amino acid sequence is identical to that of trypsin derived from porcine pancreas. Recombinant porcine trypsin exhibits the same enzymatic properties as animal-derived porcine trypsin and can be used as a substitute for pancreatic trypsin derived from pig pancreas in various biotechnological processes. The molecular weight of recombinant trypsin is 24 kDa, and its optimal pH range is 7.0-11.0. The activity of trypsin is inhibited by serine protease inhibitors such as PMSF, and metal ion chelators such as EDTA also inhibit its activity.
Application
Recombinant porcine trypsin, with the same enzymatic properties as animal-derived porcine trypsin, can be used as a substitute for pancreatic trypsin derived from pig pancreas in various biotechnological processes, including recombinant insulin production, cell culture, cell fermentation, protein digestion, and cell isolation from various tissues.
Physical Appearance
White, off-white, or pale yellow powder.
Biological Activity
≥3800 USP units/mg protein.
Unit Definition
One unit (USP) is defined as the amount of enzyme that increases the absorbance at 253 nm by 0.003 per minute, under the conditions of 25°C, pH 7.6, and a reaction volume of 3.2 mL (path length of 1 cm), using BAEE as the substrate.
Purity (Protein Electrophoresis)
A single major band.
Formulation
The Porcine Trypsin was lyophilized with mannitol as a preservative.
Recommended Usage
Dissolve in 1 mM HCl. The concentration of recombinant trypsin should be 1-10 mg/mL. The enzyme-to-substrate ratio should be 1:50-1:1000 (enzyme to target protein). The optimal pH range is 7.0-11.0.
Stability
Recombinant porcine trypsin in lyophilized powder form is stable for 24 months when stored at 2-8°C. After dissolution in 1 mM HCl or 50 mM acetic acid, the trypsin can be stored at -20°C and subjected to up to 10 freeze-thaw cycles without loss of activity.
Amino Acid Sequence
IVGGYTCAAN SIPYQVSLNS GSHFCGGSLI NSQWVVSAAH CYKSRIQVRL GEHNIDVLEG NEQFINAAKI ITHPNFNGNT LDNDIMLIKL SSPATLNSRV ATVSLPRSCA AAGTECLISG WGNTKSSGSS YPSLLQCLKA PVLSDSSCKS SYPGQITGNM ICVGFLEGGK DSCQGDSGGP VVCNGQLQGI VSWGYGCAQK NKPGVYTKVC NYVNWIQQTI AAN
Note: This amino acid sequence is for reference only; the actual length or sequence of the amino acids may vary.
Advantages
- Animal-free: Recombinant production ensures no viral contamination from external sources, and no animal-derived raw materials are used in the manufacturing process.
- Stable quality: Batch production ensures consistent and stable quality between batches.
- High purity: Higher specific activity and host protein residue content below the limit for biological products.
- Lyophilized powder: Easy storage and transportation.
Storage
Store at 4°C or lower temperature for up to two years. Since each freeze-thaw cycle can cause partial inactivation of the protein, once the corresponding concentration of the reconstitution solution is prepared, it should be divided into aliquots and stored at -20°C or lower temperature to avoid repeated freezing and thawing.
Precautions
- This product is intended for scientific research by professionals only and should not be used for clinical diagnosis or treatment. It is not for use in food or drugs and should not be stored in a regular household setting.
- For your safety and health, please wear laboratory attire and disposable gloves when handling.
Only for research and not intended for treatment of humans or animals
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