Anti-phospho-PLK1 (Thr210)(P41-65R)

Anti-phospho-PLK1 (Thr210)(P41-65R)

  • $715.00


Description :Rabbit Polyclonal Antibody

Species :Rabbit

Tag :

Expression System:

Sequence :

Specificity :Recognizes the PLK1 protein phosphorylated at threonine 201

Cited Applications :WB

Cross Reactivity :Human, Mouse, Rat, Bovine, Canine, non-Human Primate, Xenopus and Zebrafish

Host :Rabbit, IgG

Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr210 conjugated to KLH

Purification :Affinity Chromatography

Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Sample Data :Western blot of rat synaptic membrane showing specific immunolabeling of the ~66 kDa PLK1 protein phosphorylated at Thr210 (control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda-Ptase). The blot is identical to the control except that it was incubated in lambda-Ptase (1200 units for 30 min) before being exposed to the Anti-phospho-PLK1(Thr210) antibody. The immunolabeling is completely eliminated by treatment with lambda-Ptase.

Scientific Background :PLK1 is a member of the Polo-Like Kinase family of Ser/Thr kinases. PLK1 localizes to centrosomes or spindle pole bodies and undergoes subcellular relocation during the cell cycle. Deregulated activities of PLKs often result in defective centrosome duplication, maturation, and/or microtubule dynamics (1). PLKs also regulate the function of the Golgi complex. Deregulated expression of human PLK1 is strongly correlated with the development of many types of malignancies. Furthermore, ectopic expression of PLK1 dominant negative protein leads to rapid cell death (2). It has been proposed that PLK1 function is altered at different stages of mitosis through consecutive phosphorylation events at Ser137 and Thr210 (3).

References :
1. Nigg, EA. et al: Dynamic changes in nuclear architecture during mitosis: on the role of protein phosphorylation in spindle assembly and chromosome segregation. Exp Cell Res. 1996 Dec 15;229

2. Dai, W. et al: Polo-like kinases and the microtubule organization center: targets for cancer therapies. Prog Cell Cycle Res. 2003;5:327-34.

3. van de Weerdt B.C. , van Vugt MA, Lindon C, Kauw JJ, Rozendaal MJ, Klompmaker R, Wolthuis RM, Medema RH (2005) Uncoupling anaphase-promoting complex/cyclosome activity from spindle assembly checkpoint control by deregulating polo-like kinase 1. Mol. Cell Biol. Mar; 25(5):2031-44, 2005.

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Research Areas :Cancer, Cell Cycle, Ser/Thr Kinases, Cancer, Cell Cycle, Ser/Thr Kinases