Recombinant Rabbit monoclonal primary
p27 KIP 1 Recombinant Rabbit Monoclonal Antibody [SU37-04] (ET1608-61)
A431, MCF-7, human tonsil tissue, human colon carcinoma tissue, human breast carcinoma tissue, mouse lung tissue, mouse colon tissue, mouse cerebellum tissue, rat brain tissue, Hela.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
p27 KIP 1
AA408329 antibody; AI843786 antibody; Cdki1b antibody; CDKN 1B antibody; CDKN 4 antibody; CDKN1B antibody; CDKN4 antibody; CDN1B_HUMAN antibody; Cyclin Dependent Kinase Inhibitor 1B antibody; Cyclin dependent kinase inhibitor p27 antibody; Cyclin-dependent kinase inhibitor 1B (p27, Kip1) antibody; Cyclin-dependent kinase inhibitor 1B antibody; Cyclin-dependent kinase inhibitor p27 antibody; Cyclin-dependent kinase inhibitor p27 Kip1 antibody; KIP 1 antibody; KIP1 antibody; MEN1B antibody; MEN4 antibody; OTTHUMP00000195098 antibody; OTTHUMP00000195099 antibody; p27 antibody; p27 Kip1 antibody; P27-like cyclin-dependent kinase inhibitor antibody; p27Kip1 antibody
Belongs to the CDI family.
Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney.
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).
Nucleus, Cytoplasm, Endosome.
Cell cycle progression is regulated by a series of cyclin-dependent kinases consisting of catalytic subunits, designated Cdks, as well as activating subunits, designated cyclins. Orderly progression through the cell cycle requires the activation and inactivation of different cyclin-Cdks at appropriate times. A series of proteins has recently been described that function as "mitotic inhibitors." These include p21, the levels of which are elevated upon DNA damage in G1 in a p53-dependent manner; p16; and a more recently described p16-related inhibitor designated p15. A p21-related protein, p27, has been described as a negative regulator of G1 progression and speculated to function as a possible mediator of TGFβ-induced G1 arrest. p27 interacts strongly with D-type cyclins and Cdk4 in vitro and, to a lesser extent, with cyclin E and Cdk2.