Recombinant Enterkinase can specifically recognize Asp-Asp-Asp-Asp-Lys and cleave at the C-terminus of lysine residues.

Product Introduction

Enterokinase is a common serine protease that can specifically recognize the DDDDK sequence and cleave at the C-terminus of lysine residues. This product is a high-purity recombinant bovine enterokinase light chain fragment. The enzyme has high purity and specificity. It does not contain other proteases and can effectively cleave in a wide pH range (4.5-9.5) and temperature range (4-45°C).

Product Application:

1. Remove the N-terminal fusion tag of recombinant proteins, using DDDDK as the enzyme cutting site and EK enzyme digestion without residual amino acids.

2. Used to activate trypsinogen.

3. Removing the Flag tag of fusion proteins is an ideal tool for studying the structure and function of natural proteins.

4. Often used in producing and preparingrecombinant proteins and peptide drugs, such as BNP, GLP-1 and their analogs.

Product Advantages:

1. High quality: high purity, high specific activity, no residue.

2. GMP production: GMP-grade products can be provided.

3. Customized specifications: specifications can be customized according to customer quality requirement.

4. Stable supply: Stable quality control and long-term supply.

Storage:

Stored at -20℃, valid for two years.

Recommendation

1. The enzyme has high efficiency and is related to the sequence or structure of the protein to be cleaved. Doing a gradient of protein input amount before testing is recommended and then input the optimal amount.

2. High ionic strength will inhibit its activity. Under the condition of 0.25 M NaCl, it reduces the activity of rEK zymogen by about 25%; under the condition of 2 M NaCl, the activity of rEK enzyme is almost completely inhibited.

3. pH<6 or pH>9 conditions will also inhibit its activity.

4. Do not shake vigorously with vortex to avoid protein denaturation and inactivation.