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Phospho-p27Kip1-T187 Antibody Blocking PeptideSynthetic peptide

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Ordering Information
Catalog # Size Availability Price  
BP3194a 0.1 mg 400 ul In Stock $ 45.00 Add to cart
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Phospho-p27Kip1-T187 Antibody Blocking Peptide - Product info

Primary AccessionP46527
Clone Names4120752
Calculated MW22073 Da

Phospho-p27Kip1-T187 Antibody Blocking Peptide - Additional info

Gene ID 1027
Target/Specificity
The synthetic peptide sequence used to generate the antibody AP3194a was selected from the region of human Phospho-p27Kip1-T187. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format
The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
Storage
Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
Precautions
This product is for research use only. Not for use in diagnostic or therapeutic procedures.

Phospho-p27Kip1-T187 Antibody Blocking Peptide - Protein Information

Name CDKN1B
Synonyms KIP1
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 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
Cellular Location
Nucleus. Cytoplasm. Endosome (By similarity). 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 Colocalizes at the endosome with SNX6; this leads to lysosomal degradation (By similarity)
Tissue Location
Expressed in all tissues tested. Highest levels in skeletal muscle, lowest in liver and kidney

Phospho-p27Kip1-T187 Antibody Blocking Peptide - Related products

AP10418a: 27Kip1-T157 Antibody

AP13302b: CDKN1B Antibody (C-term)

AP3191a: Phospho-p27Kip1-S10 Antibody

AP3192a: Phospho-p27Kip1-S178 Antibody

AP3193a: Phospho-p27Kip1-T157 Antibody

AP3194a: Phospho-p27Kip1-T187 Antibody

AP3529a: Phospho-p27Kip1-T198 Antibody

AP6269b: 27Kip1 Antibody (C-term)

RI10983: CDKN1B predesign siRNA

LY12364a: CDKN1B Over-expression Lysate

BP10418a: 27Kip1-T157 Antibody Blocking peptide

BP3191a: Phospho-p27Kip1-S10 Antibody Blocking Peptide

BP3192a: Phospho-p27Kip1-S178 Antibody Blocking Peptide

BP3193a: Phospho-p27Kip1-T157 Antibody Blocking Peptide

BP3194a: Phospho-p27Kip1-T187 Antibody Blocking Peptide

BP3529a: Phospho-p27Kip1-T198 Antibody Blocking Peptide

BP6269b: 27Kip1 Antibody (C-term) Blocking Peptide

AT1481a: CDKN1B Antibody (monoclonal) (M01)

AO1379a: CDKN1B Antibody

AJ1569c: p27/Kip1 Antibody (C-term)

AJ1569d: p27/Kip1 Antibody Phospho (pS10)

AF1591a: KIP1 / CDKN1B (internal) Antibody

AF1769a: P27KIP1 / CDKN1B (C Terminus) Antibody

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Provided below are standard protocols that you may find useful for product applications.

BACKGROUND

p27Kip1 is 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.

REFERENCES

Kawamata, N., et al., Eur. J. Haematol. 74(5):424-429 (2005).Andreu, E.J., et al., Cancer Res. 65(8):3264-3272 (2005).Wingate, H., et al., J. Biol. Chem. 280(15):15148-15157 (2005).Wang, C., et al., J. Biol. Chem. 280(13):12339-12343 (2005).Rassidakis, G.Z., et al., Blood 105(2):827-829 (2005).