Cell Signaling Technology

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Phospho-PLK (Ser137) Biotinylated Peptide #1597

Cell Signaling Technology offers a full line of protein kinases, substrates, antibody detection reagents and HTScan® kits. Browse our "Reagents for High-Throughput Screening" product listing or contact us at drugdiscovery@cellsignal.com.

Description

This biotinylated peptide contains the residues surrounding Ser137 of PLK. The serine residue in the peptide has been chemically phosphorylated in the course of peptide synthesis. This phosphopeptide was generated for use as a positive control in CST's HTScan® kinase assay kits and kinases (HTScan® Aurora A Kinase Assay Kit #7510, HTScan® Aurora B Kinase Assay Kit #7513, HTScan® Aurora C Kinase Assay Kit #7516, HTScan® PAK4 Kinase Assay Kit #7651, HTScan® SGK3 Kinase Assay Kit #7621, HTScan® TSK2 Kinase Assay Kit #7630), but it may also serve as a positive control in other heterogeneous or homogeneous kinase assays.

Quality Control

The quality of the biotinylated peptide was evaluated by reverse-phase HPLC and by mass spectrometry.

Peptide Core Sequence

RRRS*LLE

Molecular Weight

2025 daltons

Directions for Use

This phosphorylated peptide can be detected with the Phospho-PLK (Ser137) Antibody #5070. A sample kinase assay protocol is attached.

Background

At least 4 distinct polo-like kinases exist in mammalian cells: PLK1, PLK2, PLK3 and PLK4/SAK (1). PLK1 apparently plays many roles during mitosis, particularly in regulating mitotic entry and exit. The mitosis promoting factor (MPF), cdc2/cyclin B1, is activated by dephosphorylation of cdc2 (Thr14/Tyr15) by cdc25C. PLK1 phosphorylates cdc25C at Ser198 and cyclin B1 at Ser133 causing translocation of these proteins from the cytoplasm to the nucleus (2-5). PLK1 phosphorylation of Myt1 at Ser426 and Thr495 has been proposed to inactivate Myt1, one of the kinases known to phosphorylate cdc2 at Thr14/Tyr15 (6). Polo-like kinases also phosphorylate the cohesin subunit SCC1, causing cohesin displacement from chromosome arms that allow for proper cohesin localization to centromeres (7). Mitotic exit requires activation of the anaphase promoting complex (APC) (8), a ubiquitin ligase responsible for removal of cohesin at centromeres, and degradation of securin, cyclin A, cyclin B1, Aurora A and cdc20 (9). PLK1 phosphorylation of the APC subunits Apc1, cdc16 and cdc27 has been demonstrated in vitro and has been proposed as a mechanism by which mitotic exit is regulated (10,11).

  1. Nigg, E.A. (1998) Curr. Opin. Cell Biol. 10, 776-783.
  2. Toyoshima-Morimoto, F. et al. (2002) EMBO Rep. 3, 341-348.
  3. Toyoshima-Morimoto, F. et al. (2001) Nature 410, 215-220.
  4. Peter, M. et al. (2002) EMBO Rep. 3, 551-556.
  5. Jackman, M. et al. (2003) Nat. Cell Biol. 5, 143-148.
  6. Nakajima, H. et al. (2003) J. Biol. Chem. 278, 25277-25280.
  7. Sumara, I. et al. (2002) Mol. Cell 9, 515-525.
  8. Hauf, S. et al. (2001) Science 293, 1320-1323.
  9. Peters, J.M. (1999) Exp. Cell Res. 248, 339-349.
  10. Kraft, C. et al. (2003) EMBO J. 22, 6598-6609.
  11. Kotani, S. et al. (1998) Mol. Cell 1, 371-380.

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Companion Products

This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.

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