Recombinant Enterokinase | Product Advantage |
Specificity: a specific protease, a lysine carboxy terminal site containing four aspartic acids in front is cleaved: aspartic acid-aspartic acid-aspartic acid-aspartic acid-lysine (DDDDK). is non-derived: 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: does not contain other proteases, no specific cleavage. Compliance with regulatory requirements: production equipment and production environment comply with relevant regulatory requirements, and the production process is in full compliance with NSF ISO 9001: 2015 quality system and GMP guidelines. Quality documents complete: According to customer needs, can provide relevant regulatory support documents. |
| Enzymatic Properties | Enterokinase can remove the fusion protein at the N-terminus of the protein to remove unwanted fusion tags |
| Basic Characteristics | The enzyme is purified by HPLC with high purity, high specificity and no other protease, can efficiently cleave fusion proteins over a wide pH range (4.5-9.5) and a wide temperature range. |
| Method of Use |
Reaction conditions: 25°C overnight enzyme digestion, or complete enzyme digestion takes 16-24h, with SDS-PAGE detection of enzyme digestion effect. Result Validation: Use 0.1 U of this product to cut 50 ug of fusion protein substrate, the reaction temperature is 25°C, and the enzyme cutting time gradient (8 h, 16 h, 24 h, 40 h, 48 h, 64 h) |
| Sizes | 100U; 500U; 1000U; 10KU; 100KU; 1MU |
| Cutting Sites | Enterokinase can cleave the carboxy-terminal peptide bond of lysine containing four aspartic acids: aspartic acid-aspartic acid-aspartic acid-aspartic acid-lysine (DDDDK). |
| Amino Acid Sequence | Recombinant bovine enterokinase is a highly purified recombinant bovine enterokinase light chain fragment., amino acid sequence consistent with bovine enterokinase light chain. |
| Appearance | Clear, colorless to pale yellow liquid |
| Specific Activity | ≥ 5.0 U/ml |
| Protein Electrophoresis | Single Master Strip |
| Molecular Weight (Protein Electrophoresis) | 25.8±2.6kDa |
| Warnings |
Cutting temperature: do not recommend 37°C under the condition of enzyme digestion, there may be non-specific enzyme digestion. Enzyme digestion conditions: in> 200 mM imidazole, or> 200 mM NaCl, or> 5% glycerolconditions, the effect of enzyme digestion is affected. |
| Remarks | 1U is defined as the amount of enzyme required to cleave 95% of 0.5mg of the fusion protein stored in 25mM Tris-HCl 8.0 buffer within 12h to 16h at 25°C. |
| Storage |
Storage stability: -20°C, 12 months stable; 25°C, within a week, no loss of activity. Buffer system: 50 mM Tris-HCl, pH 8.0, 250 mM NaCl, 2 mM Ca2 +, 50% glycerol. Repeated freezing and thawing 5 times, no loss of activity. |
| Transportation | Transport stability: blue ice insulation transport, stable activity. |
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