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Antigenic Specificity | PLK1 pT210, Human |
Clone | REA530 |
Host Species | Recombinant Human |
Reactive Species | human |
Isotype | IgG1 |
Format | phycoerythrin (PE) conjugate |
Size | 30 tests in 300 µL |
Concentration | 1:11 |
Applications | Intracellular flow cytometry |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | PLK1 pT210 Antibody, anti-human, PE, REAfinity™. Clone REA530 recognizes the human polo-like kinase (PLK1) antigen phosphorylated at threonine 210 (pT210). PLK1 is a key regulator of several important cell-cycle-associated processes, such as centrosome maturation, spindle assembly, sister chromatid cohesion, cytokinesis, and recovery from a DNA-damage-induced arrest. Expression of PLK1 is highly cell cycle regulated; its expression is first induced in G2 and peaks during the early stages of mitosis. PLK1 has been described to be recruited to the centrosomes in G2, as well as to spindle poles and kinetochores during mitosis. Activation of PLK1 is dependent on phosphorylation of a conserved threonine residue (T210) in the T-loop of its kinase domain. Phosphorylation of this residue starts in G2, when PLK1 activity gradually increases until it reaches its full activity when cells enter mitosis. The initial phosphorylation of T210 in G2 is mediated by the kinase Aurora-A, in concert with its cofactor Bora. Since PLK1 is highly expressed in several carcinomas, and expression is inversely correlated with the survival rate of patients in non-small cell lung, head and neck, and esophageal cancer, PLK1 is recognized as a valid prognostic marker. | Additional information: Clone REA530 displays negligible binding to Fc receptors. |
Immunogen | n/a |
Other Names | PLK-1, STPK13 |
Gene, Accession # | Gene ID: 5347 |
Catalog # | 130-108-197 |
Price | $110 |
Order / More Info | PLK1 pT210, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG |
Product Specific References | Bruinsma, W. et al. (2014) Bora and Aurora-A continue to activate Plk1 in mitosis. J. Cell. Sci. 127 (4): 801-811. | Hamanaka, R. et al. (1994) Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase. Cell Growth Differ. 5 (3): 249-257. | Kakeno, M. et al. (2014) Plk1 phosphorylates CLIP-170 and regulates its binding to microtubules for chromosome alignment. Cell Struct. Funct. 39 (1): 45-59. |