Description
Trypsin (EC 3.4.21.4) is a serine protease that specifically cleaves the peptide bonds formed at the C-terminus of lysine and arginine residues. This product is expressed in recombinant Escherichia coli and purified by chromatography. Its amino acid sequence is identical to that of trypsin derived from porcine pancreas. The manufacturing process does not use any animal-derived raw materials, ensuring no exogenous viral contamination. It can replace porcine pancreas-derived trypsin in various biotechnological applications, such as: cell culture, cell fermentation, enzymatic digestion of proteins, and cell isolation from various tissues.
This product features high purity, is free of contaminating enzymes, and meets pharmacopeial standards for residual host proteins and DNA, thereby avoiding adverse effects of impurities on cell growth. The optimal pH range is 7.0–9.0, and the pH for maximum stability is 2.0 ± 0.5.
Components
|
Components No. |
Name |
40512ES10 |
40512ES60 |
40512ES80 |
|
40512 |
PerfCell™ Recombinant Trypsin (powder) |
10 mg |
100 mg |
1 g |
Specifications
|
Cat.No. |
40512ES10 / 40512ES60 / 40512ES80 |
|
Size |
10 mg / 100 mg / 1 g |
|
Appearance |
White or off-white crystalline powder |
|
Source |
E. coli |
|
CAS |
9002-07-7 |
|
Specific Activity |
≥3800 (USP units/mg ) |
|
Purity (RP-HPLC) |
β-trypsin≥70% ,α-trypsin≤20% |
|
Activity Definition |
At 25 °C, pH 7.6, in a reaction system with a 1 cm light path, one trypsin unit (USP) is defined as the amount of enzyme that increases the absorbance at 253 nm by 0.003 per minute during hydrolysis of BAEE. |
Storage
The lyophilized recombinant trypsin powder should be stored dry at 2 °C ~ 8 °C. After reconstitution, store at –15 °C ~ –25 °C, avoid repeated freeze-thaw cycles, and protect from light. Shelf life: 2 years.
Instructions
1. This product is supplied as a lyophilized powder. Please store it immediately upon receipt under the recommended conditions described in the instructions.
2. Before opening the tube cap, it is recommended to centrifuge the tube at approximately 8,000–12,000 × g for 10–30 seconds to collect any protein adhering to the cap or tube wall to the bottom of the tube.
3. Gently dissolve the lyophilized powder by pipetting up and down or lightly shaking the vial. Do not vortex or shake vigorously to avoid protein denaturation and loss of activity.
4. The recommended working enzyme concentration is enzyme:target protein = 1:50 to 1:1000. For the optimal working concentration, please refer to relevant literature or determine and optimize experimentally based on your specific application, cell type, or animal model.
Notes
1. Activity is inhibited by serine protease inhibitors such as PMSF, and by metal ion chelators such as EDTA; high concentrations of inorganic salts may also affect enzyme activity to some extent.
2. Please operate with lab coats and disposable gloves,for your safety.
3. This product is for research use only.
FAQ
Q: How should this lyophilized powder be reconstituted? What is the recommended concentration for the stock solution?
A: This lyophilized powder is recommended to be dissolved in ddH₂O. The recommended concentration range for the stock solution is 30–100 mg/mL.
Documents
Paiement et sécurité
Vos informations de paiement sont traitées en toute sécurité. Nous ne stockons pas les détails de la carte de crédit ni accès aux informations de votre carte de crédit.
Enquête
Vous pouvez aussi aimer
FAQ
Le produit est destiné à des fins de recherche uniquement et n'est pas destiné à un usage thérapeutique ou diagnostique chez l'homme ou l'animal. Les produits et le contenu sont protégés par des brevets, des marques déposées et des droits d'auteur appartenant à Yeasen Biotechnology. Les symboles de marque indiquent le pays d'origine, pas nécessairement l'enregistrement dans toutes les régions.
Certaines applications peuvent nécessiter des droits de propriété intellectuelle tiers supplémentaires.
Yeasen se consacre à la science éthique, estimant que nos recherches doivent répondre à des questions cruciales tout en garantissant la sécurité et les normes éthiques.

