Enterokinase Protein, Bovine, Recombinant (Animal-Free, His)

Catalog No. TMPS-00026 Copy Product Info

Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site.<br/>This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.

Enterokinase Protein, Bovine, Recombinant (Animal-Free, His)

Catalog No. TMPS-00026

Copy Product Info

Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site.
This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.

Enterokinase Protein, Bovine, Recombinant (Animal-Free, His)

Pack Size	Price	USA Stock	Global Stock	Quantity
100 U	$136	7-10 days	7-10 days
500 U	$362	7-10 days	7-10 days

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For In stock only · Estimated delivery:USA Stock (1-2 days) Global Stock (5-7 days)

For research use only—not for human use. No sales to individuals. Use as intended only.

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Biological Activity	5 U/μl Unit definition: One unit is defined as the amount of enzyme sufficient to cleave 50 μg of control fusion protein (~24 kDa) in 16 hours to 95% completion at 22 °C in a buffer containing 20 mM Tris-HCl, 50 mM NaCl, 2 mM CaCl 2 , pH 7.4.
Description	Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site. This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.
Species	Bovine
Tag	His
Synonyms	PRSS7,ENTK,Enteropeptidase
Protein Purity	≥ 95% as determined by SDS-PAGE
Molecular Weight	40 kDa (Reducing conditions)
Endotoxin	< 1.0 EU/μg of protein as determined by the LAL method.
Formulation	Supplied as solution in 20 mM Tris-HCl, 200 mM NaCl, 2 mM CaCl2, 50% glycerol, pH 7.4.
Stability & Storage	Upon receiving, the product remains stable for up to 6 months at -20 °C. This product is stable for up to 1 week at 37 °C. Avoid repeated freeze-thaw cycles by making single-use aliquots before the solution is stored at -20 °C.
Shipping	Proteins are shipped with blue ice.
Research Background	Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site.

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