Cdc25C peptide is a Synthetic peptide. >97% and suitable for FuncS, HPLC.
View Alternative Names
M-phase inducer phosphatase 3, Dual specificity phosphatase Cdc25C, CDC25C
Reactivity data
Product details
ab204854 (Cdc25C peptide) can be utilized as a substrate for the following active protein kinases:
ab139629 (Active human BRSK2 full length protein)
ab60762 (Active human Chk1 full length protein)
ab69918 (Active human Chk1 full length protein)
ab119135 (Active human MARK2 full length protein)
ab60012 (Active human Mark3 full length protein)
ab105211 (Active human MARK4 full length protein)
ab179497 (Active human Serine/threonine-protein kinase NIM1 full length protein)
ab125626 (Active human ARK5 full length protein)
ab105209 (Active human NUAK2 full length protein)
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Specifications
Form
Lyophilized
General info
Function
Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle (PubMed : 8119945). When phosphorylated, highly effective in activating G2 cells into prophase (PubMed : 8119945). Directly dephosphorylates CDK1 and activates its kinase activity (PubMed : 8119945).
Sequence similarities
Belongs to the MPI phosphatase family.
Post-translational modifications
Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (PubMed:10557092). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity.
Subcellular localisation
Nucleus
Target data
Product promise
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