Recombinant Bovine Enterokinase

Mol. Wt.: 26.2 kDa（SDS-PAGE 30 kDa）

Theoretical pI: 5.20

Specific Activity: ≥40000 U/mg,1 mg rb-EK cleave at least 2000mg fusion proteins

Purity: ≥95%（SDS-PAGE）

A280nm(1 mg/mL): 2.06

Endotoxin: ≤5EU/mg

Resources: Escherichia coli (E. coli)

Storage Condition: -20℃

Storage Duration: 3 years

Description:

Enterokinase (EC 3.4.21.9) is a serine proteolytic enzyme, which can recognize the sequence of ASP ASP Lys (DDDDK) in protein efficiently and specifically, hydrolyze peptide bond at the C-terminal of lysine (Lys, K), produce cleavage, hydrolyze trypsinogen into trypsin in organism. Because enterokinase has high specificity and efficient enzymatic cleavage, it is widely used in gene engineering. Product development.

The natural enterokinase consists of a heavy chain of 115kda and a light chain of 35kDa. The heavy chain anchors the cell membrane, and the light chain has full enzyme catalytic activity. The core region of light chain activity (235A. A., 26.2kda) secreted and expressed by E.coli is more active than that of bovine enterokinase, which is especially suitable for enzyme digestion of gene engineering fusion protein.

Notes:

(1) some reagents can affect the enzyme activity, such as > 2m urea, > 250mm NaCl, > 20mm β - me, > 0.1% SDS, > 50mm imidazole. If the sample contains these components, dialysis to 50mm Tris HCl (ph8.0) is required.

(2) phosphate can inhibit the activity of enterokinase, so phosphate buffer should not be used as enzyme cutting system.

M: Protein marker standard

Lane 1: rb-EK

For research use only!