|Calculated MW||22193 Da|
|Other Names||Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, Cdkn1b|
|Target/Specificity||A synthetic peptide corresponding to residues in human p27/Kip1 was used as an 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 is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Important regulator of cell cycle progression. 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 cyclin D-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-197, 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 (By similarity). Colocalizes at the endosome with SNX6; this leads to lysosomal degradation|
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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. It is an inhibitor of cyclinE-Cdk2 complex, cyclinA-Cdk2 and cyclinD1-Cdk4 (1), and a positive regulator of cyclin D-dependent kinases such as Cdk4 (2). It plays a pivotal role in the control of cell proliferation and the loss of p27/Kip1 function may lead to carcinogenesis (4). The function of p27/Kip1 is regulated by phosphorylation and degradation events. Phosphorylation by hKIS on Serine 10 signals the nuclear export to the cytoplasm (3), while phosphorylation by Cdk2 on Threonine 187 results in ubiquitylation and degradation of p27/Kip1 (2).
1. Polyak K., et al. Cell 78:59-66, 1994. 2. The UniProt Consortium. The Universal Protein Resource (UniProt) Nucleic Acids Res. 36:D190-D195 (2008) 3. Ishida N., et al. The Journal of Biological Chemistry 277(17):14355-14358, 2002 4. Carrano,A.C., et al Nat. Cell Biol., 1, 193-199, 1999.
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