EKMax™ Enterokinase
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Invitrogen™

EKMax™ Enterokinase

EKMax™ is a recombinant preparation of the catalytic subunit of bovine enterokinase (1). EKMax™ recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleavesRead more
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Catalog NumberQuantity
E18001250 Units
E180021000 Units
Catalog number E18001
Price (USD)
1,206.00
Each
Add to cart
Quantity:
250 Units
Price (USD)
1,206.00
Each
Add to cart
EKMax™ is a recombinant preparation of the catalytic subunit of bovine enterokinase (1). EKMax™ recognizes the sequence Asp-Asp-Asp-Asp-Lys and cleaves the peptide bond after the lysine residue. The enzyme can be used to cleave any fusion protein that carries this peptide sequence (Figure 1).

Application: Removal of fusion tags from recombinant proteins.

Unit Definition: One unit of EKMax™ is the amount of enzyme required to digest 20 μg of a thioredoxin-CAT fusion protein to 90% completion in 16 hours at 37°C. One EKMax™ unit is equivalent to ∼190 trypsinogen activation units.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Product TypeEnterokinase
SpeciesCattle/Bovine
Quantity250 Units
Product LineEKMax™
Unit SizeEach
Contents & Storage
250 or 1000 units of EKMax™ is provided with 10X buffer. Store at -20°C. Guaranteed stable for 6 months when stored properly.

Frequently asked questions (FAQs)

What is the molecular weight of the EKMax enterokinase enzyme?

EKMax enterokinase is a clone of the catalytic subunit of enterokinase expressed in the yeast Pichia pastoris. The calculated molecular weight of the protein is 26.3 kDa, but it contains three sites for asparagine-linked glycosylation. The apparent molecular weight of 43 kDa is consistent with previous observations (LaVallie et al., 1993) and is assumed to be because of N-linked glycosylation.
Reference: LaVallie, E.R., Rehemtulla, A., Racie, L.A.,Diblasio, E.A., Ferenz, C., Grant, K.L. Light, A., and McCoy, J.M. (1993). Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase. J.Biol.Chem. 268, 23311-23317.

Will DTT, Triton X-100 detergent, Tween 20 detergent, Thesit, calcium chloride, sodium chloride, or SDS affect the efficiency of Enterokinase (EKMax) enzyme cleavage?

Enterokinase is active in buffers containing up to 1 mM DTT, 0.1% Triton X-100 detergent, 0.1% Tween 20 detergent, and 0.1% Thesit. It is recommended to have 10mM Tris pH 8.0 and 10 mM calcium chloride in the buffer. Enterokinase is inhibited by sodium chloride and SDS.

Should Enterokinase be resuspended in a buffer containing 50% glycerol to protect the protein from freeze/thaw cycles?

Freeze thaw has a minimal effect on the activity of Enterokinase. The addition of glycerol is not necessary but can make handling of the enzyme easier.

How specific is cleavage by EKMax Enterokinase? Are there any alternate cleavage sites for the enzyme?

Enterokinase cleaves after the sequence (Asp)4-Lys.

It has been proposed that the active center of enterokinase possesses a distinctive cationic subsite that binds -(Asp)4. Enterokinase is highly specific and tolerates very few changes to its recognition site. If the ionic charge of the recognition site is preserved, enterokinase will recognize the site, but the rate of hydrolysis of the peptide bond will be reduced (Light and Janska, 1989). The four aspartyl residues act as a signal for enterokinase cleavage. It has been reported that with only three aspartyl residues the rate of hydrolysis is reduced. Two aspartyl residues preceding the lysyl residue are the minimum number of acidic residues needed to maintain specificity (Maroux et al., 1971). Non-specific cleavage by enterokinase may occur in the cases described above, but this is usually alleviated by reducing the amount of enzyme used.

What products do you offer for enzymatic cleavage of fusion tags from recombinant proteins?

We offer the following products:

-AcTEV Protease (Cat. Nos. 12575015, 12575023)
-EKMax Enterokinase (Cat. Nos. E18001, E18002)
-SUMO Protease (Cat. No. 12588018)


Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.