• Product nameAnti-Cdc25A (phospho S75) antibody
    See all Cdc25A primary antibodies
  • Description
    Rabbit polyclonal to Cdc25A (phospho S75)
  • SpecificityDetects endogenous levels of Cdc25A only when phosphorylated at serine 75.
  • Tested applicationsSuitable for: WB, ELISAmore details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Mouse, Rat
  • Immunogen

    Synthesized phosphopeptide derived from Human Cdc25A around the phosphorylation site of serine 75 (M-G-SP-S-E).

  • Positive control
    • A2780 cell extracts.


Associated products


Our Abpromise guarantee covers the use of ab47279 in the following tested applications.

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

Application Abreviews Notes
WB 1/500 - 1/1000. Detects a band of approximately 59 kDa (predicted molecular weight: 59 kDa).
ELISA 1/10000.


  • FunctionTyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.
  • Sequence similaritiesBelongs to the MPI phosphatase family.
    Contains 1 rhodanese domain.
  • DomainThe phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction.
  • Post-translational
    Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation.
    Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization.
  • Information by UniProt
  • Database links
  • Alternative names
    • Cdc 25a antibody
    • CDC25A antibody
    • CDC25A2 antibody
    • CDC25A2 CAG isoform antibody
    • Cell division cycle 25 homolog A (S. pombe) antibody
    • Cell division cycle 25A antibody
    • Cell division cycle 25A isoform a antibody
    • Cell division cycle 25A isoform b antibody
    • D9Ertd393e antibody
    • Dual specificity phosphatase Cdc25A antibody
    • M phase inducer phosphatase 1 antibody
    • M-phase inducer phosphatase 1 antibody
    • MGC115549 antibody
    • MPIP1_HUMAN antibody
    see all

Anti-Cdc25A (phospho S75) antibody images

  • All lanes : Anti-Cdc25A (phospho S75) antibody (ab47279) at 1/500 dilution

    Lane 1 : Extracts from A2780 cells. UV + no blocking peptide.
    Lane 2 : Extracts from A2780 cells. Without UV + without blocking peptide.

    Predicted band size : 59 kDa

References for Anti-Cdc25A (phospho S75) antibody (ab47279)

This product has been referenced in:
  • Min W  et al. Poly(ADP-ribose) binding to Chk1 at stalled replication forks is required for S-phase checkpoint activation. Nat Commun 4:2993 (2013). Read more (PubMed: 24356582) »
  • Giessrigl B  et al. Hsp90 stabilizes Cdc25A and counteracts heat shock-mediated Cdc25A degradation and cell-cycle attenuation in pancreatic carcinoma cells. Hum Mol Genet 21:4615-27 (2012). Read more (PubMed: 22843495) »

See all 3 Publications for this product

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