Product nameAnti-Cdc25A (phospho S178) antibody
See all Cdc25A primary antibodies
DescriptionRabbit polyclonal to Cdc25A (phospho S178)
SpecificityDetects Cdc25A only when phosphorylated at serine 178
Tested applicationsSuitable for: WB, ELISA, IHC-Pmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic phosphopeptide derived from Human Cdc25A around the phosphorylation site of serine 178 (Q-N-SP-A-P)
- WB: extracts from UV-treated A549 cells; IHC-P: Human breast carcinoma tissue.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol, 0.87% Sodium chloride
Without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Purification notesPurified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Our Abpromise guarantee covers the use of ab79252 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/1000. Predicted molecular weight: 59 kDa.|
|IHC-P||1/50 - 1/100.|
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.
modificationsPhosphorylated 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
- Cdc 25a antibody
- CDC25A antibody
- CDC25A2 antibody
Left panel: immunohistochemistry analysis of paraffin-embedded Human breast carcinoma tissue using 1/50 ab79252. Right panel: same, after pre-incubation with the immunizing peptide.
All lanes : Anti-Cdc25A (phospho S178) antibody (ab79252) at 1/500 dilution
Lane 1 : Extracts from A549 cell treated
with UV (15mins)
Lane 2 : Extracts from A549 cell treated
with UV (15mins) with immunizing phosphopeptide at 10 µg
Lysates/proteins at 30 µg per lane.
Predicted band size: 59 kDa
Observed band size: 59 kDa
Additional bands at: 110 kDa, 117 kDa. We are unsure as to the identity of these extra bands.