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

Details for Product anti-PLK1 Antibody No. ABIN966867, Supplier: Log in to see
Antigen
  • PLK-1
  • Plx1
  • plk
  • stpk13
  • 0256/04
  • 1324/08
  • CG12306
  • Dmel\CG12306
  • PLK1
  • POLO
  • POLO/PLK1
  • Polo
  • Polo kinase
  • anon-WO0172774.3
  • l(3)01673
  • l(3)77Aa
  • l(3)S025604
  • l(3)S132408
  • PLK
  • STPK13
  • Plk
  • cb525
  • cb636
  • ik:tdsubc_2d1
  • wu:fb37g11
  • wu:fb76g03
  • xx:tdsubc_2d1
  • Snk
Alternatives
anti-Human PLK1 antibody for Enzyme Immunoassay
Epitope
pThr210
43
23
21
14
13
13
8
6
6
5
5
4
3
3
3
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
225
74
66
12
11
8
8
6
6
3
2
2
1
1
1
1
1
1
Host
Rabbit
152
69
10
Clonality
Polyclonal
Conjugate
This PLK1 antibody is un-conjugated
7
5
5
4
3
3
3
3
3
2
2
2
2
2
2
Application
Immunohistochemistry (IHC)
178
83
67
40
39
36
24
16
8
5
3
3
2
2
2
Supplier
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Supplier Product No.
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Immunogen 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)
Alternative Name PLK1 (PLK1 Antibody Abstract)
Background 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
Research Area Cancer, Cell Cycle, Kinases/Phosphatases
Pathways Cell Division Cycle
Restrictions For Research Use only
Product cited in: Wind, Kelm, Nigg et al.: "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." in: Proteomics, Vol. 2, Issue 11, pp. 1516-23, 2002 (PubMed).

Jang, Ma, Terada et al.: "Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase." in: The Journal of biological chemistry, Vol. 277, Issue 46, pp. 44115-20, 2002 (PubMed).

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

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

Golsteyn, Schultz, Bartek et al.: "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, Vol. 107 ( Pt 6), pp. 1509-17, 1994 (PubMed).

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

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