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MilliporeSigma

ENTK-RO

Roche

Enterokinase

from calf intestine

Sinónimos:

restriction protease enterokinase

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352204

biological source

bovine (calf) intestine

form

lyophilized

mol wt

150 kDa

packaging

pkg of 3 × 250 μg (11351311001)
pkg of 3 × 30 μg (11334115001)

manufacturer/tradename

Roche

concentration

1:50 % (w/w)

optimum pH

8

storage temp.

2-8°C

General description

Enterokinase is a  protease from calf intestine and supplied in a quality optimized for the cleavage of fusion proteins.
Enterokinase is a heterodimeric serine protease involved in the conversion of trypsinogen to trypsin. It cleaves trypsinogen by highly specific manner at the trypsinogen activation peptide site following the sequence (A~p)~-L and stimulates its physiological activities.

Specificity

Serine protease acting as a restriction protease that recognizes the amino acid sequence -(Asp)4-Lys-X. The aspartic acid residues can be partially substituted by glutamic acid.

Application

Quality
Purity: highly purified, not standardized with albumin
Quality control: function tested
Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. For the processing of recombinant proteins, the desired protein is fused with Enterokinase  recognition sequence. After purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase.

Preparation Note

Working concentration: 1:50 (w/w)
Storage conditions (working solution): A solution of enterokinase, stored at 2 to 8 °C, can be used up to one week.

Other Notes

For life science research only. Not for use in diagnostic procedures.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


Certificados de análisis (COA)

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Visite la Librería de documentos

E R LaVallie et al.
The Journal of biological chemistry, 268(31), 23311-23317 (1993-11-05)
Enterokinase (enteropeptidase) is a heterodimeric serine protease that is responsible for the physiological activation of trypsinogen by highly specific cleavage of the trypsinogen activation peptide following the sequence (Asp)4-Lys. In this paper, we report the cloning and functional expression of

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