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anti-Human PLK1 Antibodies:
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Human Polyclonal PLK1 Primary Antibody for IHC - ABIN966866
Lake, Jelinek: Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase. in Molecular and cellular biology 1994
Show all 7 Pubmed References
Human Polyclonal PLK1 Primary Antibody for IHC - ABIN966867
Golsteyn, Schultz, Bartek, Ziemiecki, Ried, Nigg: Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. in Journal of cell science 1994
Show all 7 Pubmed References
Human Monoclonal PLK1 Primary Antibody for WB - ABIN967616
Ando, Ozaki, Yamamoto, Furuya, Hosoda, Hayashi, Fukuzawa, Nakagawara: Polo-like kinase 1 (Plk1) inhibits p53 function by physical interaction and phosphorylation. in The Journal of biological chemistry 2004
Show all 3 Pubmed References
Human Monoclonal PLK1 Primary Antibody for FACS, IHC - ABIN1098105
Lin, Sun, Wang: Suppression of Polo like kinase 1 (PLK1) by p21(Waf1) mediates the p53-dependent prevention of caspase-independent mitotic death. in Cellular signalling 2011
Show all 3 Pubmed References
Xenopus laevis Polyclonal PLK1 Primary Antibody for WB - ABIN152619
Kumagai, Dunphy: Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts. in Science (New York, N.Y.) 1996
Show all 3 Pubmed References
Human Monoclonal PLK1 Primary Antibody for ICC, ELISA - ABIN969580
Lee, Rhee: PLK1 phosphorylation of pericentrin initiates centrosome maturation at the onset of mitosis. in The Journal of cell biology 2011
Show all 2 Pubmed References
Human Polyclonal PLK1 Primary Antibody for ICC, IF - ABIN256400
Seeger-Nukpezah, Liebau, Höpker, Lamkemeyer, Benzing, Golemis, Schermer: The centrosomal kinase Plk1 localizes to the transition zone of primary cilia and induces phosphorylation of nephrocystin-1. in PLoS ONE 2012
Show all 2 Pubmed References
Human Polyclonal PLK1 Primary Antibody for IHC (p), WB - ABIN392446
Negishi, Kumano, Nishida: Polo-like kinase 1 is required for localization of Posterior End Mark protein to the centrosome-attracting body and unequal cleavages in ascidian embryos. in Development, growth & differentiation 2011
Show all 2 Pubmed References
Human Monoclonal PLK1 Primary Antibody for ICS - ABIN1177152
Jang, Ma, Terada, Erikson: Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase. in The Journal of biological chemistry 2002
Human Monoclonal PLK1 Primary Antibody for ICS - ABIN1177154
Peter, Gleixner, Cerny-Reiterer, Herrmann, Winter, Hadzijusufovic, Ferenc, Schuch, Mirkina, Horny, Pickl, Müllauer, Willmann, Valent: Polo-like kinase-1 as a novel target in neoplastic mast cells: demonstration of growth-inhibitory effects of small interfering RNA and the Polo-like kinase-1 targeting drug BI 2536. in Haematologica 2011
Study shows that cnn exon1A-encoded proteins interact with Polo at 2 residues and that this interaction is required for polar body and pericentriolar matrix formation in syncytial embryos.
Cdk1 (show CDK1 Antibodies) phosphorylates the conserved centriole protein Sas-4 during mitosis. This creates a Polo-docking site that helps recruit Polo to daughter centrioles.
Polo is an important in vivo regulator of the pathological functions of APP (show APP Antibodies).
Both conditions impaired NSC lineage progression. Ca(2 (show CA2 Antibodies)) mito homeostasis is influenced by Polo-mediated phosphorylation of a conserved residue in Miro
During pericentriolar matrix formation exon 1A Cnn-Long Form proteins likely bind Polo kinase before phosphorylation by Polo for Cnn transport to the centrosome.
Polo kinase is required for localization and activity of the chromosomal passenger complex in mitosis and meiosis.
Centrioles, which usually separate during the anaphase of the first meiosis, remained held together in a V-shaped configuration suggesting that Polo kinase regulates the proteolysis that breaks centriole linkage to ensure their disengagement.
Results show that Polo kinase positively and negatively regulates Augmin distribution for microtubule nucleation and acentrosomal spindle formation.
Regulation of Polo by Aurora B (show AURKB Antibodies) and Map205 is required for cytokinesis.
These data indicate APC (show APC Antibodies)(Cort (show CORT Antibodies)) ubiquitylates Mtrm at the oocyte-to-embryo transition, thus preventing excessive inhibition of Polo kinase activity due to Mtrm's presence.
Novel roles for Plk and GSK3 regulation of ADAM13 (show ADAM33 Antibodies) function in cranial neural crest cell migration.
Plx1-mediated degradation of Bora in interphase generates oscillations in Plx1 activity and is essential for development.
Coordinated interplays between Plx1 and Gwl (show MASTL Antibodies) are required for reactivation of these kinases from the G(2)/M DNA damage checkpoint and efficient checkpoint recovery.
the penultimate CRS (show CARS Antibodies) serine (Ser (show SIGLEC1 Antibodies) 101) of cyclin b1 (show CCNB1 Antibodies) is a Plx substrate
Results suggest that polo-like kinase (Plx1) could be the missing regulator that prevents maturation-promoting factor autoamplification in stage IV oocytes.
Plx1 cooperates with CaMKII (show CAMK2G Antibodies) to regulate cyclosome regulators, and is necessary for release of cytostatic factor metaphase arrest and sufficient when overexpressed.
Data show that Plx1 couples tension signals to cellular responses through phosphorylation of the 3F3 (show TRIM32 Antibodies)/2 epitope and targeting structural and checkpoint proteins to kinetochores.
Polo-like kinase Plx1 is an essential factor for calcium ion-induced meiotic exit during cytostatic factor arrest
Polo-like kinase (Plx1) phosphorylates xTRF1 in vitro and the mitotic xTRF1-chromatin association was significantly impaired when Plx1 was immunodepleted from the extracts (Plx1).
Cdk1 (show CDK1 Antibodies) phosphorylation of BubR1 (show BUB1B Antibodies) controls spindle checkpoint arrest and plk-mediated formation of the 3F3 (show TRIM32 Antibodies)/2 epitope.
findings thus elucidate a critical role for Plk1 in CyclinB1-Cdk1 (show CDK1 Antibodies) activation and mitotic entry and outline how CyclinA2-Cdk (show CDK4 Antibodies), an S-promoting factor, poises cells for commitment to mitosis.
Data show that a microRNA-mimic to increase miR (show MLXIP Antibodies)-34a together with siRNA to silence PLK1 oncogene (show RAB1A Antibodies) prolonged survival.
PLK1 inhibitors may be effective for patients with high-risk or relapsed neuroblastomas with upregulated PLK1.
The authors found that SYP (show SYP Antibodies)-4 is phosphorylated dependent on Polo-like kinases PLK-1/2. They propose a model in which Polo-like kinases recognize crossover designation and phosphorylate SYP (show SYP Antibodies)-4 thereby stabilizing the synaptonemal complex and making chromosomes less permissive for further double-strand break formation.
Data suggest that FBXW7 (show FBXW7 Antibodies), MCL1 (show MCL1 Antibodies) and PLK1 may be relevant predictive markers of tumor progression and response to paclitaxel treatment.
we have identified lnc-RI as a new regulator of mitosis which acts by releasing PLK1 mRNA activity via competition for binding to miRNA-210-3p.
A FAK (show PTK2 Antibodies)-Src (show SRC Antibodies) signaling pathway downstream of integrin-mediated cell adhesion was found to decelerate both PLK1 degradation and CEP55 (show CEP55 Antibodies) accumulation at the midbody. These data identify the regulation of PLK1 and CEP55 (show CEP55 Antibodies) as steps where integrins exert control over the cytokinetic abscission.
Data indicate that the mitotic kinase Polo-like kinase 1 (PLK1) was an important effector of S1P (show MBTPS1 Antibodies)-S1P5 (show S1PR5 Antibodies) signaling, and a new function of the SphK1 (show SPHK1 Antibodies)-S1P (show MBTPS1 Antibodies) pathway specifically in the control of mitosis in HeLa cells.
identified Polo-like kinase 1 (PLK1), a major signaling hub in the spindle subnetwork, as phosphorylated at the conserved Tyr (show TYR Antibodies)(217) in the kinase domain. Substitution of Tyr (show TYR Antibodies)(217) with a phosphomimetic residue eliminated PLK1 activity in vitro and in cells.
PLK1 inhibition mitigates autophagy in cancer cells both under nutrient starvation and sufficiency, and a role of PLK1 in autophagy is also observed in the invertebrate model organism Caenorhabditis elegans.
Plk1 plays an essential role during the meiosis I/meiosis II transition in porcine oocytes, and the regulation is associated with Plk1's effects on homologous chromosome segregation in the Anaphase-telophase I stage.
Thus, these results indicated that Plk1 is essential for porcine embryos to complete the first mitotic division. Furthermore, Plk1 regulation was associated with effects on spindle assembly and chromosome arrangement
PLK1 might play a critical role in vascular smooth muscle cell mitosis in hyperplastic intima of the injured vessels.
Data show that Polo-like kinase 1 is activated before M phase promoting factor (MPF (show MSLN Antibodies)), which is consistent with its role in activating MPF (show MSLN Antibodies) in mammalian oocytes.
CIP2A (show KIAA1524 Antibodies) acts as a scaffold for CEP192-mediated microtubule organizing center assembly by recruiting Plk1 and aurora A (show AURKA Antibodies) during meiotic maturation in mouse oocytes
Plk1 overexpression may contribute to tumor formation by both inducing chromosomal instability and suppressing the DDR (show DDR1 Antibodies) pathway.
Plk1 is essential for the mammalian embryonic development, and its depletion leads to mitotic alterations and lethality at different stages during mammalian development.
Plk1 regulated angiotensin II-dependent activation of RhoA (show RHOA Antibodies) and actomyosin dynamics in VSMCs in a mitosis-independent manner. This regulation depended on Plk1 kinase activity. Plk1 haploinsufficiency in mice did not induce obvious cell proliferation defects but did result in arterial structural alterations, which frequently led to aortic rupture and death.
The findings reveal a PLK1-Fbw7 (show FBXW7 Antibodies)-Myc (show MYC Antibodies) signaling circuit that underlies tumorigenesis and validate PLK1 inhibitors, alone or with Bcl2 (show BCL2 Antibodies) antagonists, as potential effective therapeutics for MYC (show MYC Antibodies)-overexpressing cancers.
These data implicate the insulin (show INS Antibodies)-FoxM1 (show FOXM1 Antibodies)/PLK1/CENP-A (show CENPA Antibodies) pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes.
centrosome maturation occurs during interphase in an MLK (show MUSK Antibodies)-dependent manner, independent of the classic mitotic kinase, Plk1.
centrosome protein Dzip1 (show DZIP1 Antibodies) mediates the assembly of the BBSome-Dzip1 (show DZIP1 Antibodies)-PCM1 (show MBD1 Antibodies) complex in the centriolar satellites (CS) at the G0 phase for ciliary translocation of the BBSome. Phosphorylation of Dzip1 (show DZIP1 Antibodies) at Ser (show SIGLEC1 Antibodies)-210 by Plk1 (polo-like kinase 1) during the G2 phase promotes disassembly of this complex, resulting in removal of Dzip1 (show DZIP1 Antibodies) and the BBSome from the CS.
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin (show VIM Antibodies) phosphorylation at Ser (show SIGLEC1 Antibodies)-56.
Results indicate that polo-like kinase 1 (PLK1) controls the onset of spindle assembly and spindle formation, and is essential for anaphase-promoting complex/cyclosome (APC (show APC Antibodies)/C) activation before anaphase onset in zygotes.
Report the 2.3-A crystal structure of the complex of the N-terminal kinase domain (KD) and a C-terminal Polo-box domain (PBD together with a PBD-binding motif of Drosophila melanogaster microtubule-associated protein (show FAM82A2 Antibodies) 205 (Map205(PBM)).
Studies demonstrate that Plk1 is required for embryonic proliferation because its activity is crucial for mitotic integrity.
for the first time that Plk1 can accommodate extended ATP-competitive compounds that project toward the adaptive pocket and help the enzyme order its activation segment
These results reveal a crucial and conserved role of phosphorylation of the N terminus of Bora for Plk1 activation and mitotic entry.
Our data further show that PLK-1 is needed for nuclear envelope breakdown during early embryogenesis
PLK-1 substitutes for Mps1 in controlling spindle checkpoint initiation in C. elegans.
NCAPG2 (show NCAPG2 Antibodies) plays an important role in regulating proper chromosome segregation through a functional interaction with PLK1 during mitosis
CDK-1 (show CDK1 Antibodies) activates PLK-1 via SPAT (show AGXT Antibodies)-1 phosphorylation to promote entry into mitosis.
The result provide key insights into the regulation of homolog pairing and reveal that targeting of plk-1 to the NE by meiotic chromosomes establishes the conserved linkages to cytoskeletal forces needed for homology assessment.
SPAT (show AGXT Antibodies)-1 and PLK-1 depletion causes impaired polarity with abnormal length of the anterior and posterior PAR (show AFG3L2 Antibodies) domains, and partial plk-1(RNAi) or spat (show AGXT Antibodies)-1(RNAi), but not air-1(RNAi), can rescue the lethality of a par-2 (show F2RL1 Antibodies) mutant.
Polo kinases, via their polo box domains, bind to and regulate the activity of two key polarity proteins, MEX-5 and MEX (show ZSWIM2 Antibodies)-6.
plk-1 asymmetry contributes to asynchronous cell division in C. elegans embryos.
human homolog catalyzes the phosphorylation of a Golgi reassembly stacking protein (GRASP65); may play a role in Golgi apparatus fragmentation and reorganization during mitosis
serine/threonine-protein kinase PLK1
, polo kinase
, polo protein kinase
, cell cycle regulated protein kinase
, polo (Drosophia)-like kinase
, polo like kinase
, serine/threonine-protein kinase 13
, polo-like protein kinase
, polo-like kinase homolog
, polo-like kinase 1
, serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase SNK
, serum-inducible kinase