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. 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); while phosphorylation by hKIS on Serine 10 signals the nuclear export to the cytoplasm.
Product Information
Format
Culture Supernatant
Control
MCF-7 cell lysate.
Presentation
Unpurified rabbit monoclonal IgG in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Applications
Application
Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target. Detect p27(Kip1) using this Anti-p27(Kip1) Antibody, clone Y236 validated for use in WB, FC, IP, IC, IH.
Key Applications
Immunohistochemistry
Western Blotting
Flow Cytometry
Immunoprecipitation
Immunocytochemistry
Application Notes
Immunocytochemistry: A 1:100-250 dilution of a previous lot was used in IC.
Immunohistochemistry: A 1:100-250 dilution of a previous lot was used in IH.
Immunoprecipitation: A 1:50 dilution of a previous lot was used in IP.
Flow Cytometry: A 1:40 dilution of a previous lot was used in FC.
Biological Information
Immunogen
Synthetic peptide corresponding to the C-terminus of human p27 (Kip1).
Epitope
C-terminus
Clone
Y236
Host
Rabbit
Specificity
This antibody recognizes p27(Kip1) at the C-terminus.
Isotype
IgG
Species Reactivity
Rat Human
Species Reactivity Note
Proven to react with Human and Rat. Not expected to react with Mouse.
This gene encodes a cyclin-dependent kinase inhibitor, which shares a limited similarity with CDK inhibitor CDKN1A/p21. The encoded protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and thus controls the cell cycle progression at G1. The degradation of this protein, which is triggered by its CDK dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state. [provided by RefSeq]
Function:Important regulator of cell cycle progrssion. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Positive regulator of cyclin D-dependent kinases such as CDK4. Regulated by phosphorylation and degradation events. Subunit structure:Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated p27kip1. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to p27KIP degradation. Interacts with SPDYA in the SPDYA/CDK2/p27kip1 complex. Interacts (Thr-198 phosphorylated-form) with 14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to the cytoplasm. Interacts with AKT1, LYN and UHMK1; the interactions lead to cytoplasmic mislocation, phosphorylation of p27kip1 and inhibition of cell cycle arrest. Interacts (unphosphorylated form) with CDK2. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction induces nuclear translocation. Interacts with GRB2. Subcellular location:Nucleus. Cytoplasm. 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. Tissue specificity: Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney. Induction:Maximal levels in quiescence cells and early G(1). Levels decrease after mitogen stimulation as cells progress toward S-phase. Domain:A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity. Post-translational modification: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 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 KPC1/KPC2 complex and, in the nucleus, by SCF/SKP2. The latter requires prior phosphorylation on Thr-187. Ref.5 Involvement in disease:Defects in CDKN1B are the cause of multiple endocrine neoplasia type 4 (MEN4) [MIM:610755]. Multiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2. Ref.16 Miscellaneous:Decreased levels of p27Kip1, mainly due to proteosomal degradation, are found in various epithelial tumors originating from lung, breast, colon, ovary, esophagus, thyroid and prostate. Sequence similarities:Belongs to the CDI family.
Product Usage Statements
Quality Assurance
Routinely evaluated by western blot on MCF-7 cell lysate.
Western Blot Analysis: A 1:1,000-1:2,000 dilution of this lot was used to detect p27(Kip1) in MCF-7 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
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. 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); while phosphorylation by hKIS on Serine 10 signals the nuclear export to the cytoplasm.
Product Information
Format
Culture Supernatant
Control
MCF-7 cell lysate.
Presentation
Unpurified rabbit monoclonal IgG in buffer containing 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Applications
Application
Please note that this product will not be available for sale after March 15, 2015. Please select one of the other antibodies against this target. Detect p27(Kip1) using this Anti-p27(Kip1) Antibody, clone Y236 validated for use in WB, FC, IP, IC, IH.
Key Applications
Immunohistochemistry
Western Blotting
Flow Cytometry
Immunoprecipitation
Immunocytochemistry
Application Notes
Immunocytochemistry: A 1:100-250 dilution of a previous lot was used in IC.
Immunohistochemistry: A 1:100-250 dilution of a previous lot was used in IH.
Immunoprecipitation: A 1:50 dilution of a previous lot was used in IP.
Flow Cytometry: A 1:40 dilution of a previous lot was used in FC.
Biological Information
Immunogen
Synthetic peptide corresponding to the C-terminus of human p27 (Kip1).
Epitope
C-terminus
Clone
Y236
Host
Rabbit
Specificity
This antibody recognizes p27(Kip1) at the C-terminus.
Isotype
IgG
Species Reactivity
Rat Human
Species Reactivity Note
Proven to react with Human and Rat. Not expected to react with Mouse.
This gene encodes a cyclin-dependent kinase inhibitor, which shares a limited similarity with CDK inhibitor CDKN1A/p21. The encoded protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and thus controls the cell cycle progression at G1. The degradation of this protein, which is triggered by its CDK dependent phosphorylation and subsequent ubiquitination by SCF complexes, is required for the cellular transition from quiescence to the proliferative state. [provided by RefSeq]
Function:Important regulator of cell cycle progrssion. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Positive regulator of cyclin D-dependent kinases such as CDK4. Regulated by phosphorylation and degradation events. Subunit structure:Interacts with NUP50; the interaction leads to nuclear import and degradation of phosphorylated p27kip1. Interacts with COPS5, subunit of the COP9 signalosome complex; the interaction leads to p27KIP degradation. Interacts with SPDYA in the SPDYA/CDK2/p27kip1 complex. Interacts (Thr-198 phosphorylated-form) with 14-3-3 proteins, binds strongly YWHAQ, weakly YWHAE and YWHAH, but not YWHAB nor YWHAZ; the interaction with YWHAQ results in translocation to the cytoplasm. Interacts with AKT1, LYN and UHMK1; the interactions lead to cytoplasmic mislocation, phosphorylation of p27kip1 and inhibition of cell cycle arrest. Interacts (unphosphorylated form) with CDK2. Interacts (phosphorylated on Tyr-88 and Tyr-89) with CDK4; the interaction induces nuclear translocation. Interacts with GRB2. Subcellular location:Nucleus. Cytoplasm. 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. Tissue specificity: Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney. Induction:Maximal levels in quiescence cells and early G(1). Levels decrease after mitogen stimulation as cells progress toward S-phase. Domain:A peptide sequence containing only AA 28-79 retains substantial Kip1 cyclin A/CDK2 inhibitory activity. Post-translational modification: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 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 KPC1/KPC2 complex and, in the nucleus, by SCF/SKP2. The latter requires prior phosphorylation on Thr-187. Ref.5 Involvement in disease:Defects in CDKN1B are the cause of multiple endocrine neoplasia type 4 (MEN4) [MIM:610755]. Multiple endocrine neoplasia (MEN) syndromes are inherited cancer syndromes of the thyroid. MEN4 is a MEN-like syndrome with a phenotypic overlap of both MEN1 and MEN2. Ref.16 Miscellaneous:Decreased levels of p27Kip1, mainly due to proteosomal degradation, are found in various epithelial tumors originating from lung, breast, colon, ovary, esophagus, thyroid and prostate. Sequence similarities:Belongs to the CDI family.
Product Usage Statements
Quality Assurance
Routinely evaluated by western blot on MCF-7 cell lysate.
Western Blot Analysis: A 1:1,000-1:2,000 dilution of this lot was used to detect p27(Kip1) in MCF-7 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
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