In eukaryotic cells, mitosis is initiated following the activation of a protein kinase known variously as maturation-promoting factor, M-phase specific histone kinase or M-phase kinase. This protein kinase is composed of a catalytic subunit (Cdc2), a regulatory subunit (cyclin B) and a low molecular weight subunit (p13 SUC1). The Cdc/cyclin enzyme is subject to multiple levels of control of which the regulation of the catalytic subunit by tyrosine phosphorylation is the best understood. Tyrosine phosphorylation inhibits the Cdc2/cyclin B enzyme and tyrosine dephosphorylation, occurring at the onset of mitosis, directly activates the pre-MPF complex. Evidence has estalished that B-type cyclins not only act on M-phase regulatory subunits of the Cdc2 protein kinase, but also activate the Cdc25A and Cdc25B endogenous tyrosine phosphatase, of which Cdc2 is the physiological substrate. The specificity of this effect is shown by the inability of either cyclin A or cyclin D1 to display any such stimulation of Cdc25A or Cdc25B.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Formulierung:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
