Cdc2, an evolutionarily conserved serine/threonine-specific protein kinase, is essential in the cell cycle transition from G2 to M phase. Cdc2 is regulated by association with B-type cyclins and by reversible phosophorylation. Cyclin B binding facilitates the phosphorylation of Cdc2 p34 on three regulatory sites: threonine 14, tyrosine 15, and threonine 161. In higher eukaryotes, Cdc2 is negatively regulated by phosphorylation of two residues located in the ATP-binding site, Thr 14 and Tyr 15. Cdc2 is positively regulated by the cyclin-dependent phosphorylation of Thr 161. Both phosphorylation and de- phosphorylation at Thr 161 are required for progression through the cell cycle.

Cyclin-dependent kinase 1; Cell division control protein 2 homolog; Cell division protein kinase 1; p34 protein kinase; CDK1; CDC2; CDC28A; CDKN1; P34CDC2

p06493

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 34 kDa

Rabbit

This antibody detects endogenous levels of Cdk1/Cdc2 protein only when phosphorylated at Thr14.

Synthetic phosphopeptide derived from human Cdk1/Cdc2 around the phosphorylation site of Threonine 14.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.