Render Target: STATIC
Render Timestamp: 2024-12-26T11:35:07.524Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:23:43.045
Product last modified at: 2024-05-30T07:10:38.675Z
Cell Signaling Technology Logo
1% for the planet logo
PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PLK4 Antibody #3258

Filter:
  • WB
  • IF

Inquiry Info. # 3258

Please see our recommended alternatives.

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 95
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunofluorescence (Immunocytochemistry) 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PLK4 Antibody detects endogenous levels of total PLK4 protein.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Cys458 of human PLK4. Antibodies were purified by peptide affinity chromatography.

    Background

    At least four 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).

    Substitution of Thr210 with Asp has been reported to elevate PLK1 kinase activity and delay/arrest cells in mitosis, while a Ser137Asp substitution leads to S-phase arrest (12). In addition, while DNA damage has been found to inhibit PLK1 kinase activity, the Thr210Asp mutant is resistant to this inhibition (13). PLK1 has been reported to be phosphorylated in vivo at Ser137 and Thr210 in mitosis; DNA damage prevents phosphorylation at these sites (14).

    PLK4/SAK is transcriptionally repressed by p53 and may contribute to p53-mediated apoptosis (12). PLK4 has also been identified as a key regulator of centriole duplication (13-15).
    1. Nigg, E.A. (1998) Curr Opin Cell Biol 10, 776-83.
    2. Toyoshima-Morimoto, F. et al. (2002) EMBO Rep 3, 341-8.
    3. Toyoshima-Morimoto, F. et al. (2001) Nature 410, 215-20.
    4. Peter, M. et al. (2002) EMBO Rep 3, 551-6.
    5. Jackman, M. et al. (2003) Nat Cell Biol 5, 143-8.
    6. Nakajima, H. et al. (2003) J Biol Chem 278, 25277-80.
    7. Sumara, I. et al. (2002) Mol Cell 9, 515-25.
    8. Hauf, S. et al. (2001) Science 293, 1320-3.
    9. Peters, J.M. (1999) Exp. Cell Res. 248, 339-49.
    10. Kraft, C. et al. (2003) EMBO J 22, 6598-609.
    11. Kotani, S. et al. (1998) Mol Cell 1, 371-80.
    12. Jang, Y.J. et al. (2002) J Biol Chem 277, 44115-20.
    13. Smits, V.A. et al. (2000) Nat Cell Biol 2, 672-6.
    14. Tsvetkov, L. and Stern, D.F. (2005) Cell Cycle 4, 166-71.
    15. Li, J. et al. (2005) Neoplasia 7, 312-323.
    16. Habedanck, R. et al. (2005) Nat. Cell Biol. 7, 1140-1146.
    17. Ko, M.A. et al. (2005) Nat. Genet. 37, 883-888.
    18. Bettencourt-Dias, M. et al. (2005) Curr. Biol. 15, 2199-2207.
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    Alexa Fluor is a registered trademark of Life Technologies Corporation.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.