Recombinant Enterokinase is a high-purity recombinant fragment of bovine enterokinase light chain, with an amino acid sequence identical to that of the bovine enterokinase light chain. It has the same specific cleavage site as naturally extracted enterokinase, which is Asp-Asp-Asp-Asp-Lys (DDDDK). It can be used to remove fusion proteins located at the N-terminus of proteins to remove unwanted fusion tags, ensuring the accurate N-terminal sequence of recombinant fusion proteins. At the same time, Recombinant Enterokinase has higher cutting activity than natural enzymes.

Recombinant Enterokinase, His Tag is a high-purity, high-activity, and highly specific bovine enterokinase expressed by Pichia pastoris secretion. It can effectively cleave fusion proteins within a wide pH range (4.5-9.5) and a wide temperature range, and still has partial activity under various detergents and denaturants. This product has a His tag, which can be easily removed through Ni²⁺ affinity column after the cutting reaction, greatly simplifying the subsequent purification process.

Features

• Strong specificity—A specific protease that cuts the carboxyl terminus of lysine containing four aspartic acids in front: Asp-Asp-Asp-Asp-Lys.
• High purity—No other protease,No non-specific cutting.
• Animal free—Recombinantly produced, free from exogenous viral contamination, and no animal-derived materials are used in the production process.
• Quality Stability: Batch production ensures stable and continuous batch manufacturing; there are no differences between product batches, ensuring consistent quality.
• Adequate Capacity: Yeasen possesses fermenters ranging from 5L to 1500L, meeting the varying batch requirements of different clients at different stages.

Applications

• In the production process of fusion peptides and proteins, it is used to remove fusion proteins located at the N-terminus of proteins to remove unwanted fusion tags, ensuring the accurate N-terminal sequence of recombinant fusion proteins.
• In the field of biopharmaceuticals, the production and preparation of GLP-1 analog peptide drugs are commonly used, such as semaglutide and liraglutide.

Specifications

Molecular Weight: *Due to the glycosylation effect after expression in Pichia pastoris, the molecular weight of the target protein shown by SDS-PAGE is about 40 kDa.

Activity Definition：*The cleavage efficiency may vary depending on the substrate. Generally, smaller proteins tend to have higher cleavage efficiency. The enzyme activity defined by Yeasen is based on a large protein with a molecular weight of approximately 64.6 kDa. For oligopeptide substrates, it can generally reach a maximum of 1 unit to cleave 500 μg.

Components

Storage

The product can be stored at -25 ~ -15℃ for one year.

Documents:

Safety Data Sheet

20395_MSDS_HB250609.pdf

Manuals 

20395_Manuals_Ver. HB250609.pdf