Maternal embryonic leucine zipper kinase (KIAA0175, HPK38) or MELK, a new member of the Snf1/AMPK family of kinases, encodes a protein with a kinase catalytic domain and a leucine zipper motif consisting of a periodic repetition of leucine residues at every seventh residue located within the N-terminal catalytic domain. This motif has been observed in myriad DNA-binding proteins and is presumed to be involved in protein-DNA interactions, and potentially protein-protein interactions. Research predicts that the gene product of MELK plays a role in the signal transduction events in the egg and early embryo. Mouse and human MELK proteins share 95% sequence identity in the kinase domain and northern blot analysis in mouse indicates that MELK expression is restricted to spermatogonia in the testis and to oocytes in the ovary.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
MELK (N449) polyclonal antibody detects endogenous levels of MELK protein.
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