太鼎生物科技/太鼎食安科技

Enterokinase, cleavage enzyme 100U  

Enterokinase

Description

The enterokinase included in this kit is
the catalytic subunit of the native holoenzyme, and is highly active and
specific for cleaving fusion proteins with the recognition sequence, DDDDK, in
the interdomain linker.

Because this product is produced from mammalian expression system, it is highly
glycosylated and shows extremely specific cleavage activity compared to other
E. coli produced enterokinases. The purified enterokinase behaves as a 47kD
band under denaturing and reducing conditions as visualized on SDS-PAGE.

Applications

Enterokinase is a site-specific protease
that recognizes and cleaves after the C-terminal end of lysine residue in the
recognition sequence, DDDDK. Unlike other site-specific proteases that cut
within the recognition sequences leaving extra amino acids in the cleaved
peptide products, the C-terminal peptide fragment produced from the
enterokinase cleavage reaction doesn't inherent any residues from the DDDDK
recognition sequence*. Therefore, the application can be extremely advantageous
for producing a 100% native protein sequence and structure from recombinant
fusion protein,




















which has the desired product immediately after the
enterokinase recognition sequence, DDDDK. [*Note: Enterokinase will not cleave
at site when lysine is followed by proline.]

In addition, DDDDK is part of the octapeptide FLAG tag (DYKDDDDK), which has
been used as a fusion tag for recognition by antibody and detection of fusion
protein expression with Western blot analysis, and for purification of the
fusion protein by Anti-FLAG affinity chromatography. This array of applications
makes enterokinase an ideal tool in the research involving the study of protein
structure and function, and protein production where native protein structures
and sequences are desired.

Components

·  Enterokinase: 100
units in 100ul ***One unit of enterokinase will cleave 50µg of cleavage control
protein to 95% completion in 16hrs at 25°C.***

Special Features

·  No residues left
from recognition sequence after cleavage.

·  Produced in
mammalian expression system.

·  Allows removal of
tags after use in purification.

·  Excellent price.

Data Sheet

References

·  Baratti, J.,
Maroux, S., and Louvard, D. (1973). Effect of Ionic Strength and Calcium Ions
on the Activation of Trypsinogen by Enterokinase. A Modified Test for the
Quantitative Evaluation of the Enzyme. Biochem. Biophys. Acta 321: 632-638.

·  Choi, S.I., Song,
H.W., Moon, J.W., and Seong, B.L. (2001). Recombinant Enterokinase Light Chain
with Affinity Tag: Expression from Saccharomyces cerevisiae and Its Utilities
in Fusion Protein Technology. Biotechnol. Bioeng. 75: 718-724.

·  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.

·  Lu, D., Fűtterer,
K., Korolev, S., Zheng, X., Tan, K., Waksman, G., and Sadler, J.E. (1999)
Crystal Structure of Enteropeptidase Light Chain Complexed with an Analog of
the Trypsinogen Activation Peptide. J. Mol. Biol. 292: 361-373.

·  Maroux, S.,
Baratti, J., and Desnuelle, P. (1971). Purification and Specificity of Porcine
Enterokinase. J. Biol. Chem. 246: 5031-5039.

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