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

[Note]: Cleavage efficiency may vary depending on the substrate. Smaller proteins are generally cleaved more efficiently. The enzyme activity is defined using a ~64.6 kDa substrate. For small peptide substrates, cleavage efficiency may reach up to 1 U per 500 μg of substrate.

Components

Shipping and Storage

This product should be stored at -25~-15℃ for 2 years.

Application

Removal of N-terminal fusion tags from recombinant proteins to ensure accurate protein sequences.

Widely used in the biopharmaceutical field, including the production of GLP-1 analog peptide drugs.

Figures

1. High Specificity

Figure 1. Yeasen Enterokinase (Cat#20396ES) demonstrates superior cleavage performance compared to Supplier N*.

2. Strong Stability

Figure 2. Stability of Yeasen enterokinase (Cat#20396ES) under repeated freeze–thaw cycles and accelerated storage conditions. Enzyme activity remained stable with no significant loss.

Two randomly selected batches of Yeasen enterokinase (Cat#20396ES) were tested. After 10 and 20 freeze–thaw cycles, enzyme activity showed no significant change compared with the initial activity. Similarly, storage at 25 °C for 7, 16, and 32 days, and at 37 °C for 7 and 14 days, showed no significant reduction in activity.

Documents:

Safety Data Sheet

20396_MSDS_HB250825_EN.PDF

Manuals

20396_Manual_Ver.EN20250825.pdf