Recombinant Enterokinase (rEK) is a highly purified recombinant fragment of bovine enterokinase light chain. Its amino acid sequence is identical to that of the native bovine enterokinase light chain, providing the same substrate specificity as naturally extracted enterokinase. The cleavage site is Asp-Asp-Asp-Asp-Lys (DDDDK), which enables removal of fusion tags located at the N-terminus of recombinant proteins, ensuring accurate N-terminal sequence of the target protein. Additionally, recombinant enterokinase exhibits higher catalytic activity compared to its natural counterpart. GMP-grade Recombinant Enterokinase (with His-tag) is a high-purity, high-activity, and highly specific bovine enterokinase produced via secretion expression in Pichia pastoris. Manufactured under GMP-compliant processes, this enzyme effectively cleaves fusion proteins over a broad pH range (4.5–9.5) and a wide temperature range, and retains partial activity even in the presence of various detergents and denaturing agents. The enzyme contains a His-tag, allowing easy removal after the cleavage reaction using a Ni²⁺ affinity column, significantly simplifying downstream purification procedures. Features High Specificity: A specific protease that cleaves at the carboxyl terminus of lysine following four aspartic acid residues: Asp-Asp-Asp-Asp-Lys (DDDDK). High Purity: Free from other proteases; no non-specific cleavage observed. Non-animal Origin: Recombinantly produced, free from exogenous viral contamination; no animal-derived materials used during production. Consistent Quality: Batch production ensures stable and continuous supply with minimal lot-to-lot variation. High Production Capacity: YEASEN possesses fermentation systems ranging from 5 L to 1500 L, capable of meeting diverse customer demands across different development and production stages. Multiple Grade Options: R&D Grade (Cat# 20395ES) and GMP Grade (Cat# 20396ES). GMP-grade products are manufactured under ISO 13485 quality management system and are supported with comprehensive quality documentation. Specifications Source Recombinantly expressed in Pichia pastoris Molecular Weight Theoretical: 22.7 kDa Note: Due to glycosylation in Pichia expression, the apparent molecular weight on SDS-PAGE is approximately 40 kDa. Appearance Sterile liquid Storage Buffer 50 mM Tris-HCl, 250 mM NaCl, 2 mM CaCl₂, 50% Glycerol, pH 8.0 Enzyme Concentration 5 U/μL Purity ≥95% Endotoxin
