p27 (Kip1) is a cyclin-dependent kinase inhibitor (cdkI) that associates with cyclin/cdk complexes to inhibit their catalytic activity. p27 was
first identified as a result of its role in TGF-β-induced G1 phase arrest and cell-cell contact. In vitro, p27 binds tightly to cyclin D-Cdk4, cyclin
E-Cdk2, and cyclin A-Cdk2 complexes to inhibit their activity. In non-dividing cells, the level of p27 is elevated and its activity gradually
decreases as cells reach S phase. Mitogenic stimulation causes the cyclin D-CDK complex to bind and sequester p27. An increase in Cdk2
activity during G1 causes the degradation of p27. Phosphorylation of p27 is necessary for its degradation and is mediated by the SCF complex
[Skp1,2/Cdc53 (cullins)]/F-box proteins. SCF complexes are involved in targeting phosphorylated proteins for ubiquitin-dependent
proteolysis. The antibodies recognize mouse p27. A peptide coupled to KLH and corresponding to amino acids 184-197 at the C-terminus of
mouse p27 was used as immunogen.
原厂资料：
注意事项：
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
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