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Production of Full-Length, Biologically Active MEK1WT and MEK1CA

Useful tools for signal transduction research and drug screening


Quinn Lu Chao-Feng Zheng
Stratagene Cloning Systems, Inc.


Stratagene has successfully expressed and purified recombinant, wild-type human MEK1WT and a constitutively active mutant (MEK1CA) using the ESP yeast protein expression and purification system. These MEKs, produced in yeast, are full length and undegraded, whereas MEKs produced in E. coli are significantly degraded. Wild-type MEK1WT can be used as a substrate for upstream MEK activators, such as Raf, MEKK or mos. The uses for constitutively active MEK1CA include identifying potential substrates, making activated MAPK, screening for inhibitors and performing microinjection studies.

The term mitogen-activated protein kinase/extracellular signal-activated protein kinase (MAPK/ERK kinase, MEK) refers to two dual-specificity protein kinases that phosphorylate and thereby activate both threonine and tyrosine residues of mitogen-activated protein kinases (MAPK).1-3 In order to be fully active, MEK itself needs to be phosphorylated on two serine residues by other protein kinases, such as raf.4-6 The recombinant human MEKs produced in E. coli are not very active because E. coli lacks MEK activators. Substitution of the two phosphoacceptors (Ser-218 and Ser-222) in MEK1WT with glutamic acid, in combination with an internal deletion (from amino acid 32 to amino acid 51), produced a mutant MEK that is more active than wild type.4-6 This mutant, made by site-directed mutagenesis, is referred to as constitutively active MEK1 (MEK1CA) and does not need to be activated by other protein kinases.

Recombinant MEK1WT and MEK1CA are very useful tools for signal transductio
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