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% purity and suitable for SDS-PAGE, MS.
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
M G S S H H H H H H S S G L V P R G S H M S N V R V S N G S P S L E R M D A R Q A E H P K P S A C R N L F G P V D H E E L T R D L E K H C R D M E E A S Q R K W N F D F Q N H K P L E G K Y E W Q E V E K G S L P E F Y Y R P P R P P K G A C K V P A Q E S Q D V S G S R P A A P L I G A P A N S E D T H L V D P K T D P S D S Q T G L A E Q C A G I R K R P A T D D S S T Q N K R A N R T E E N V S D G S P N A G S V E Q T P K K P G L R R R Q T
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Select an associated product type
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.
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, p27, KIP1
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% purity and suitable for SDS-PAGE, MS.
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, p27, KIP1
>90% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, MS
No
No
Human
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.32% Tris HCl
M G S S H H H H H H S S G L V P R G S H M S N V R V S N G S P S L E R M D A R Q A E H P K P S A C R N L F G P V D H E E L T R D L E K H C R D M E E A S Q R K W N F D F Q N H K P L E G K Y E W Q E V E K G S L P E F Y Y R P P R P P K G A C K V P A Q E S Q D V S G S R P A A P L I G A P A N S E D T H L V D P K T D P S D S Q T G L A E Q C A G I R K R P A T D D S S T Q N K R A N R T E E N V S D G S P N A G S V E Q T P K K P G L R R R Q T
Full Length
24.2 kDa
1 to 198
Recombinant
His tag N-Terminus
Liquid
ab113602 was purified using conventional chromatography.
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.
Belongs to the CDI family.
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.
Nucleus, Endosome
Blue Ice
1-2 weeks
+4°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
The protein known as p27 KIP1 also referred to as p27 CDKN1B or KIP1 is a member of the kinase inhibitory protein family. It plays an important role in cell cycle regulation by inhibiting cyclin-dependent kinases (CDKs). p27 KIP1 weighs approximately 27 kDa and can be found in various tissues where it regulates cell proliferation. The protein functions as a suppressor by binding to cyclin-CDK complexes preventing the transition from G1 phase to S phase in the cell division cycle.
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.
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.
Dysfunction of p27 KIP1 has links to cancer and neurodegenerative diseases. Low levels or mutations can lead to uncontrolled cell proliferation contributing to the development and progression of cancers such as breast cancer. p27 KIP1's role in neurodegenerative diseases involves its regulation of neuronal cell cycle re-entry with abnormalities potentially exacerbating conditions like Alzheimer's disease. In these contexts its interaction with proteins such as cyclin E and CDK2 becomes particularly relevant in understanding disease mechanisms.
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15% SDS-PAGE analysis of ab113602 (3μg)
3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
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