PLK1 anticorps (Polo-Like Kinase 1) (pThr210)

Details for Product anti-PLK1 Antibody No. ABIN966867, Fournisseur: Connectez-vous pour afficher
Antigène
  • PLK
  • STPK13
  • plk
  • PLK-1
  • Plx1
  • stpk13
  • Plk
  • cb525
  • cb636
  • ik:tdsubc_2d1
  • wu:fb37g11
  • wu:fb76g03
  • xx:tdsubc_2d1
  • polo like kinase 1
  • polo like kinase 1 S homeolog
  • polo-like kinase 1
  • polo-like kinase 1 (Drosophila)
  • Serine/threonine-protein kinase plk-1
  • PLK1
  • plk1.S
  • plk1
  • Plk1
  • plk-1
Épitope
pThr210
48
39
22
17
15
15
12
9
7
7
6
6
5
4
3
3
3
3
3
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivité
Humain, Souris, Rat (Rattus)
353
155
90
64
20
18
12
12
11
7
3
3
3
3
2
2
1
1
1
1
1
1
Hôte
Lapin
188
171
17
Clonalité
Polyclonal
Conjugué
Cet anticorp PLK1 est non-conjugé
13
11
11
9
9
9
8
6
6
6
6
6
6
6
6
6
5
4
3
2
2
2
2
2
2
2
2
2
Application
Immunohistochemistry (IHC)
313
182
104
78
70
45
44
34
27
5
4
4
3
3
2
2
2
Options
Fournisseur
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N° du produit (Fournisseur)
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Immunogène Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to Nresidues of human PLK1(Serine/threonine-protein kinase PLK1) (Polo-like kinase 1)
Autre désignation PLK1 (PLK1 Antibody Extrait)
Sujet PLK1(Serine/threonine-protein kinase) that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of APC/C inhibitors, and the regulation of mitotic exit and cytokinesis. PLK1 is activated by serine and threonine phosphorylation. PLK1 interacts with CEP170 and EVI5. PLK1 interacts and phosphorylates ERCC6L. PLK1 accumulates to a maximum during the G2 and M phases, declines to a nearly undetectable level following mitosis and throughout G1 phase, and then begins to accumulate again during S phase. Autophosphorylation and phosphorylation of Ser-137 are not significant events during activation of PLK1 in M phase.
Synonyms: PLK
Pathways Cycle Cellulaire, M Phase
Restrictions For Research Use only
Produit citée dans: Jang, Ma, Terada, Erikson: "Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase." dans: The Journal of biological chemistry, Vol. 277, Issue 46, pp. 44115-20, 2002 (PubMed).

Wind, Kelm, Nigg, Lehmann: "Identification of phosphorylation sites in the polo-like kinases Plx1 and Plk1 by a novel strategy based on element and electrospray high resolution mass spectrometry." dans: Proteomics, Vol. 2, Issue 11, pp. 1516-23, 2002 (PubMed).

Uchiumi, Longo, Ferris: "Cell cycle regulation of the human polo-like kinase (PLK) promoter." dans: The Journal of biological chemistry, Vol. 272, Issue 14, pp. 9166-74, 1997 (PubMed).

Lee, Erikson: "Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures." dans: Molecular and cellular biology, Vol. 17, Issue 6, pp. 3408-17, 1997 (PubMed).

Bräuninger, Strebhardt, Rübsamen-Waigmann: "Identification and functional characterization of the human and murine polo-like kinase (Plk) promoter." dans: Oncogene, Vol. 11, Issue 9, pp. 1793-800, 1995 (PubMed).

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." dans: Journal of cell science, Vol. 107 ( Pt 6), pp. 1509-17, 1994 (PubMed).

Background publications Lake, Jelinek: "Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase." dans: Molecular and cellular biology, Vol. 13, Issue 12, pp. 7793-801, 1994 (PubMed).

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