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  • Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains.

Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains.

European journal of biochemistry (1993-04-15)
D S Dorow, L Devereux, E Dietzsch, T De Kretser
ABSTRACT

Using the polymerase chain reaction to study mRNA expressed in human epithelial tumor cells, a member of a new family of protein kinases was identified. The catalytic domain of this kinase has amino-acid-sequence similarity to both the Tyr-specific and the Ser/Thr-specific kinase classes. Clones representing two members of this new family have been isolated from a human colonic epithelial cDNA library and sequenced. The predicted amino-acid sequences of these clones reveal that, in addition to the unusual nature of their kinase catalytic domains, they contain two Leu/Ile-zipper motifs and a basic sequence, near their C-termini. As they possess domains associated with proteins from two distinct functional groups, these kinases have been named mixed-lineage kinases (MLK) 1 and 2. mRNA from MLK1 has been found to be expressed in epithelial tumor cell lines of colonic, breast and esophageal origin. The MLK1 gene has been mapped to human chromosome 14q24.3-31.

MATERIALS
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Product Description

Sigma-Aldrich
MLK1 (1-433), active, GST tagged human, PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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