• NatureRecombinant
  • SourceBaculovirus infected Sf9 cells
  • Amino Acid Sequence
    • SpeciesHuman


Our Abpromise guarantee covers the use of ab51426 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activitySpecific activity 17nmol/min/mg.
  • Applications

    Western blot

    Functional Studies


  • FormLiquid
  • Additional notes

    ab91090 (Cow Casein full length protein) can be utilized as a substrate for assessing Kinase activity

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 25% Glycerol, 50mM Sodium phosphate, 300mM Sodium chloride, 0.2mM DTT, 0.1mM PMSF, pH 7.0

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • Cell cycle regulated protein kinase
    • PLK
    • PLK 1
    • PLK-1
    • plk1
    • PLK1_HUMAN
    • Polo like kinase 1
    • Polo-like kinase 1
    • Serine/threonine protein kinase 13
    • Serine/threonine protein kinase PLK1
    • Serine/threonine-protein kinase 13
    • Serine/threonine-protein kinase PLK1
    • STPK 13
    • STPK13
    see all
  • FunctionSerine/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. Required for recovery after DNA damage checkpoint and entry into mitosis. Required for kinetochore localization of BUB1B. Phosphorylates SGOL1. Required for spindle pole localization of isoform 3 of SGOL1 and plays a role in regulating its centriole cohesion function. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Regulates TP53 stability through phosphorylation of TOPORS.
  • Tissue specificityPlacenta and colon.
  • Sequence similaritiesBelongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.
    Contains 2 POLO box domains.
    Contains 1 protein kinase domain.
  • Developmental stageAccumulates 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.
  • Post-translational
    Catalytic activity is enhanced by phosphorylation of Thr-210. Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase.
    Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint.
    Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) in anaphase and following DNA damage, leading to its degradation by the proteasome. Ubiquitination is mediated via its interaction with FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry into mitosis and is essential to maintain an efficient G2 DNA damage checkpoint.
  • Cellular localizationNucleus. Chromosome > centromere > kinetochore. Cytoplasm > cytoskeleton > centrosome. During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGOL1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization.
  • Information by UniProt

Recombinant human PLK1 protein images

  • Kinase activity assay. Specific activity 17 nmol/min/mg.
  • Recombiant human PLK1 protein (His tagged). Molecular weight 70 kDa.

References for Recombinant human PLK1 protein (ab51426)

ab51426 has not yet been referenced specifically in any publications.

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