The antiserum was produced against synthesized peptide derived from human WEE1 around the phosphorylation site of Ser53. AA range:19-68

Phospho-Wee 1 (S53) Polyclonal Antibody detects endogenous levels of Wee 1 protein only when phosphorylated at S53.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):EDsAF

WEE1

Wee1-like protein kinase

WEE1 ;
Wee1-like protein kinase ;
WEE1hu ;
Wee1A kinase

WEE1 G2 checkpoint kinase(WEE1) Homo sapiens This gene encodes a nuclear protein, which is a tyrosine kinase belonging to the Ser/Thr family of protein kinases. This protein catalyzes the inhibitory tyrosine phosphorylation of CDC2/cyclin B kinase, and appears to coordinate the transition between DNA replication and mitosis by protecting the nucleus from cytoplasmically activated CDC2 kinase. [provided by RefSeq, Jul 2008],

Catalytic activity:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.,cofactor:Binds 2 magnesium ions per subunit.,enzyme regulation:Synthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during m phase. Protein levels fall in M phase as a result of decreased synthesis combined with degradation. Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location.,Function:May act as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDC2 before the onset of mitosis. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation. Specifically phosphorylates and inactivates cyclin B1-complexed CDC2 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDC2 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDC2 does not occur.,PTM:Phosphorylated during M and G1 phases. Also autophosphorylated.,PTM:Ubiquitinated and degraded at the onset of G2/M phase.,similarity:Belongs to the protein kinase superfamily.,similarity:Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.,similarity:Contains 1 protein kinase domain.,

Nucleus.

Amygdala,Blood,Epithelium,Human uterus endothel primary cell culture,Placenta,Skin,

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