Proteinase K (solution)
Enzyme for digesting proteins in biological samples. Form: solution, concentration 20 mg/ml, activity ≥ 30 U/mg.
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Description
Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. Enterokinase will not work if the recognition site is followed by a proline.
Full Name
Enterokinase
Source
E. coli
Species
Bovine
Accession #
P98072
Molecule Weight
Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain with 235 a.a. and a 6-his tag. It has a predicted molecular mass of 27 kDa.
Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1 EU per μg of the protein as determined by the LAL method
Unit Definition: One unit is defined as the amount of enzyme needed to cleave 50 μg of fusion protein in 16 hours to 95% completion at 22°C in a buffer containing 25mM Tris-HCl, pH 8.0.
Biological Activity
100 IU/μg
Storage
rbEK remains stable up to 1 year at -20°C from date of receipt. It will remain stable at 37°C for one week without losing any activity. Please avoid freeze-thaw cycles. Avoid repeated freeze-thaw cycles.
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Enzyme for digesting proteins in biological samples. Form: solution, concentration 20 mg/ml, activity ≥ 30 U/mg.
Human Trypsin 1, encoded by the PRSS1 gene, is also known as cationic trypsinogen. It contains a signal peptide (residues 1‑15), a pro region (residues 16‑23), and a mature chain (residues 24‑247).
Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion.
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