The Cyclin Dependent Kinase Inhibitor Antibody Sampler Kit provides an economical means to investigate cyclin dependent kinase inhibitors. The kit contains enough primary and secondary antibody to perform four western blot experiments.
Each antibody in the Cyclin Dependent Kinase Inhibitor Sampler Kit detects endogenous levels of its respective target protein and does not cross-react with other family members.
Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues within the amino terminus of p15, the carboxy terminus of human p16 or the carboxy terminus of p57. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with synthetic peptides corresponding to residues within the carboxy terminus of human p21, the amino terminus of p27 (#3686), and recombinant p27 (#3698).
The cyclin-dependent kinase complex can exist as an active, binary complex containing cyclin and kinase or as an inactive, ternary complex when the pair associates with a CKI inhibitor. Some of these component proteins act selectively within their cyclin/CDK complex while other proteins exhibit a broader range of functions, including roles apart from the CDK complex (1,2). The INK4 family is characterized by 32 amino acid ankyrin repeats that mediate specific interactions with CDK4/6 and cyclinD/CDK4/6 (3). The Kip family includes p27, perhaps one of the most versatile proteins by virtue of its inherently context-adaptive structure. p27 has been implicated in regulatory roles of cell cycle progression, malignant transformation, cell motility, and differentiation (4,5). Similarly, p21 interacts with several CDK complexes during different cell cycle stages to exert different effects; p21 is regulated by phosphorylation and ubiquitin-mediated degradation (6,7).
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc. U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
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