The Cdc2/cyclin B enzyme, involved in regulation of mitosis in eukaryotic cells, is subject to multiple levels of control. Among these, the regulation of the catalytic subunit by Tyrosine phosphorylation is the best understood. Tyrosine phosphorylation inhibits the Cdc2/cyclin B complex, while Tyrosine dephosphorylation, which occurs at the onset of mitosis, directly activates the pre-MPH complex. The Cdc25 gene serves as a rate-limiting mitotic activator, apparently due to its action as the Cdc2 Tyrosine phosphatase. In the absence of Cdc25, Cdc2 accumulates in a Tyrosine phosphorylated state. In addition, Cdc25 proteins from a variety of species have been shown to share a low degree of sequence similarity with other Tyrosine phosphatases. The Cdc25 gene family consists of at least three members that share approximately 40% identity in their most conserved carboxy-terminal sequences. Human Cdc25B may be phosphorylated on Ser 187, an event that inactivates Cdc25B activity.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
See 1 citations for p-Cdc25BAntibody (Ser 187 )
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Ser 187 phosphorylated Cdc25B of human origin by WB IP IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of Ser 187 phosphorylated Cdc25B of human origin by WB, IP, IF, IHC(P) and ELISA