|Tested species reactivity||Human, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phosphopeptide derived from human Cyclin B1 around the phosphorylation site of Serine 126|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.2|
|Contains||15mM sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:200|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody detects endogenous protein at a molecular weight of 60 kDa.
Purity is >95% by SDS-PAGE.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.