Recombinant Human p27 KIP 1 protein
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Recombinant Human p27 KIP 1 protein is a Human Full Length protein, in the 1 to 198 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
KIP1, p27, CDKN1B, Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human p27 KIP 1 protein (AB113602)
15% SDS-PAGE analysis of ab113602 (3μg)
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human p27 KIP 1 protein (AB113602)
3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
Reactivity data
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We recommend this product because it’s often used in the same experiment or related research.
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Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The function of p27 KIP1 involves its role in controlling cell growth and division. It achieves this by becoming a part of larger protein complexes involving CDKs and cyclins. By directly interacting with these complexes p27 KIP1 modulates cell cycle progression therefore acting as a brake on cellular proliferation. The protein is important in maintaining proper cell cycle checkpoints and preventing uncontrolled cell growth which is essential for normal cellular functioning.
Pathways
The involvement of p27 KIP1 centers on cell cycle regulation and signaling pathways such as the PI3K/AKT pathway. Its interaction with CDKs and cyclins situates it within the core mechanisms that determine cell division timing. p27 KIP1 operates alongside other proteins like cyclin D and CDK4/6 fitting into the regulatory intricacies of these pathways. Proper functioning of these pathways ensures cellular homeostasis and prevents the development of oncogenic processes.
Specifications
Form
Liquid
Additional notes
ab113602 was purified using conventional chromatography.
General info
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.
Sequence similarities
Belongs to the CDI family.
Post-translational modifications
Phosphorylated; phosphorylation occurs on serine, threonine and tyrosine residues. Phosphorylation on Ser-10 is the major site of phosphorylation in resting cells, takes place at the G(0)-G(1) phase and leads to protein stability. Phosphorylation on other sites is greatly enhanced by mitogens, growth factors, cMYC and in certain cancer cell lines. The phosphorylated form found in the cytoplasm is inactivate. Phosphorylation on Thr-198 is required for interaction with 14-3-3 proteins. Phosphorylation on Thr-187, by CDK1 and CDK2 leads to protein ubiquitination and proteasomal degradation. Tyrosine phosphorylation promotes this process. Phosphorylation by PKB/AKT1 can be suppressed by LY294002, an inhibitor of the catalytic subunit of PI3K. Phosphorylation on Tyr-88 and Tyr-89 has no effect on binding CDK2, but is required for binding CDK4. Dephosphorylated on tyrosine residues by G-CSF.. Ubiquitinated; in the cytoplasm by the KPC complex (composed of RNF123/KPC1 and UBAC1/KPC2) and, in the nucleus, by SCF(SKP2). The latter requires prior phosphorylation on Thr-187. Ubiquitinated; by a TRIM21-containing SCF(SKP2)-like complex; leads to its degradation.. Subject to degradation in the lysosome. Interaction with SNX6 promotes lysosomal degradation (By similarity).
Subcellular localisation
Nucleus
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