Western blot of rat synaptic membrane showing specific immunolabeling of the ~66 kD PLK protein phosphorylated at Thr210 (control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: L-Ptase). The blot is identical to the control except that it was incubated in L-Ptase (1200 units for 30 min) before being exposed to the phospho-Thr210 PLK antibody. The immunolabeling is completely eliminated by treatment with L-Ptase.
|Tested species reactivity||Human, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Immunogen is surrounding Tyr210 of PLK1|
|Storage buffer||PBS with 50% glycerol|
|Storage Conditions||Maintain refrigerated at 2-8°C for up to 1 month. For long term storage store at -20°C|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1,000|
* 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.
Considerable evidence indicates that a Polo-Like Kinase (PLK) plays an important role in cell cycle regulation. PLK is also required for bipolar spindle formation, activation of the anaphase-promoting complex/cyclosome, and cytokinesis. Recent work led to the identification of a PLKK that is thought to be responsible for activation of PLK. Recent work (Erikson, et al., 2004) has shown that PLKK is in turn activated by phosphorylation at three sites (Ser482, Ser486 and Ser490). Thus activation of PLK is thought to involve a kinase cascade involving the phosphorylation of Ser482,486,490 in PLKK.
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