Recombinant Enterokinase (rEK) is a highly pure fragment of the recombinant bovine enterokinase light chain. Its amino acid sequence is identical to that of the bovine enterokinase light chain, featuring enzymatic cleavage sites that are as specific as those found in naturally extracted enterokinase, with cutting sites at Asp-Asp-Asp-Asp-Lys. This enables the removal of the fusion protein located at the N-terminus of the protein, eliminating unnecessary fusion tags. Additionally, rEK exhibits higher cleavage activity compared to the natural enzyme. The Recombinant Enterokinase is a high-purity, highly active, and highly specific bovine enterokinase produced through recombinant expression in Escherichia coli. Devoid of other proteases, it can effectively cleave fusion proteins over a broad pH range (4.5-9.5) and a wide temperature range. It retains partial activity even in the presence of various detergents and denaturing agents. This product is label-free, and due to its extremely high enzymatic cleavage activity, minimal amounts are needed for cleavage reactions, ensuring no interference with downstream protein applications, making removal unnecessary. Feature Specificity: The enzyme exhibits specificity for a particular amino acid sequence, cleaving at the carboxyl-terminal site containing four aspartic acids followed by lysine (DDDDK). Animal free: Produced through recombinant methods, ensuring no contamination from exogenous viruses. The production process does not involve any animal-derived materials. Quality stability: Batch production guarantees consistently stable batches, with no variations in quality between different batches. High purity: Devoid of other proteases, ensuring non-specific cleavage. Compliance with regulations: Production facilities and environments adhere to relevant regulatory requirements. The manufacturing process adheres to GMP guidelines. Comprehensive quality documentation: Can provide relevant regulatory support documents as per customer requirements. Specification Source Expressed in E.coli. Molecular Weight 25.85 kDa Appearance Clear, colorless liquid. Concentration ≥5 U/uL Activity Definition One unit of activity is defined as the amount of enzyme required to cleave 95% of 500 μg of a 30KD fusion protein containing enterokinase cleavage sites, under the following conditions: 25°C, 12-16 hours, in a buffer system consisting of 25 mM Tris-HCl, pH 8.0. Endotoxin ＜1 EU/μg HCP ≤0.01% Tag No Storage Buffer 50 mM Tris-HCl，pH8.0，250 mM NaCl，2 mM CaCl2，50% Glycerol The amount of recombinant protein cleaved per unit of Enterokinase (EK) Suppliers Yeasen 5 U/μL Thermo 1 U/μL NEB 16 U/μL Activity 500 μg/U 20 μg/U 25 μg/U Storage Store at -25 to -15°C for 1 years. Documents: Safety Data Sheet 20401ES-MSDS-HB250225.PDF Manuals 20401_Manual_Ver. EN20250225_EN.pdf
