|Application ||WB, IHC, IF|
|Calculated MW||22073 Da|
|Other Names||Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1|
|Target/Specificity||A synthetic peptide corresponding to residues in the C-term of human p27(Kip1) was used as immunogen|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||p27/Kip1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A- CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry.|
|Cellular Location||Nucleus. Cytoplasm. Endosome. Note=Nuclear and cytoplasmic in quiescent cells. AKT- or RSK- mediated phosphorylation on Thr-198, binds 14-3-3, translocates to the cytoplasm and promotes cell cycle progression. Mitogen- activated UHMK1 phosphorylation on Ser-10 also results in translocation to the cytoplasm and cell cycle progression Phosphorylation on Ser-10 facilitates nuclear export. Translocates to the nucleus on phosphorylation of Tyr-88 and Tyr-89 Colocalizes at the endosome with SNX6; this leads to lysosomal degradation (By similarity).|
|Tissue Location||Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney|
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Provided below are standard protocols that you may find useful for product applications.
p27(Kip1) is a cyclin-dependent kinase inhibitor involved in G1 arrest. p27(Kip1) binds to and inhibits cyclinE-Cdk2 complex, cyclinA-CDK2 and cyclinD1-CDK4 (1). p27(Kip1) is regulated by phosphorylation on serine 10 (S10) and threonine 187 (T187). Phosphorylation by CDK2 on T187 results in ubiquitylation and degradation of p27(Kip1) (2); while phosphorylation by hKIS on S10 signals the nuclear export to the cytoplasm (3).
1. Polyak K., Lee M.-H., Erdjument-Bromage H., Koff A., Roberts J.M., Tempst P., Massague J.; Cell 78:59-66 (1994).
2. Carrano,A.C., Eytan,E., Hershko,A. and Pagano,M. (1999) SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol., 1, 193-199
3. Rodier,G., Montagnoli,A., Di Marcotullio,L., Coulombe,P., Draetta,G.F., Pagano,M. and Meloche,S. (2001). EMBO J., 20, 6672-6682
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