Description
Recombinant Bovine 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 Bovine enterokinase has higher cutting activity than natural enzymes.
Recombinant Bovine Enterokinase, His, Expressed in Yeast 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.
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Features
1. Strong specificity—A specific protease that cuts the carboxyl terminus of lysine containing four aspartic acids in front: Asp-Asp-Asp-Asp-Lys.
2. High purity—No other protease,No non-specific cutting.
3. Animal free—Recombinantly produced, free from exogenous viral contamination, and no animal-derived materials are used in the production process.
4.Quality Stability: Batch production ensures stable and continuous batch manufacturing; there are no differences between product batches, ensuring consistent quality.
5. Adequate Capacity: A 500L fermenter can yield approximately 50 MU of enterokinase, and Yeasen possesses fermenters ranging from 5L to 1500L, meeting the varying batch requirements of different clients at different stages.
Applications
l 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.
Specifications
|
Source |
Yeast recombinant expression |
|
Molecular Weight* |
Theoretical value 22.7 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% |
|
Activity Definition |
One unit of activity is defined as the amount of enzyme required to cut 95% of the 500 μg fusion protein with enterokinase cleavage site under the condition of 25°C, 12-16 hours, in a 25 mM Tris-HCl buffer system, pH 8.0. |
*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.
Storage
The product can be stored at -25 ~ -15℃ for one year.
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