Cell division cycle protein 27 homolog (760-771)

Cell division cycle protein 27 homolog

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-193

Synonyms/Alias:Cell division cycle protein 27 homolog (760-771)

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Sequence
FSWAMDLDPKGA
Areas of Interest
Antigen-presenting Cells; Cancer Research

Cell division cycle protein 27 homolog (760-771) is a synthetic peptide fragment derived from the C-terminal region of the CDC27 protein, a conserved component of the anaphase-promoting complex/cyclosome (APC/C). As a crucial regulator of cell cycle progression, CDC27 is involved in ubiquitin-mediated proteolysis of key mitotic substrates, thereby orchestrating the orderly transition between different cell cycle phases. The 760-771 amino acid segment represents a functionally relevant motif within the larger CDC27 sequence, making it a valuable tool for dissecting protein-protein interactions, post-translational modifications, and regulatory mechanisms underpinning mitotic control. The availability of this defined peptide fragment enables researchers to explore the structural and biochemical properties of CDC27 in a controlled and reproducible manner.

Protein interaction studies: The CDC27 (760-771) peptide serves as a targeted probe for investigating direct binding interactions with APC/C subunits, regulatory factors, or substrate recognition motifs. By employing this fragment in in vitro binding assays, pull-down experiments, or affinity chromatography, researchers can map interaction interfaces, assess binding affinities, and characterize the molecular determinants governing APC/C assembly and substrate specificity. This approach provides mechanistic insight into how the C-terminal domain of CDC27 contributes to the integrity and function of the APC/C complex.

Phosphorylation and post-translational modification analysis: The defined sequence of the 760-771 region allows for precise examination of phosphorylation events or other post-translational modifications that modulate CDC27 function. Utilizing synthetic peptides as substrates in kinase assays or mass spectrometry-based studies enables the identification of modification sites, the determination of specific modifying enzymes, and the assessment of functional consequences on APC/C activity. These studies are instrumental in elucidating regulatory checkpoints that control cell cycle transitions and mitotic fidelity.

Antibody production and epitope mapping: The CDC27 (760-771) peptide is frequently used as an immunogen for generating sequence-specific antibodies or as a reference standard in epitope mapping applications. Custom antibodies raised against this peptide segment can selectively recognize CDC27 in immunoblotting, immunoprecipitation, or immunofluorescence experiments, facilitating the detection and quantification of the protein in diverse biological samples. Epitope mapping with this peptide also aids in defining antibody specificity and cross-reactivity, supporting the development of high-quality immunological reagents.

Peptide competition and functional inhibition assays: In functional studies of APC/C-mediated ubiquitination, the CDC27 (760-771) peptide can act as a competitive inhibitor or decoy substrate, enabling researchers to dissect the contribution of the C-terminal motif to complex activity. By introducing the peptide into cell-free systems or reconstituted APC/C assays, it is possible to probe the effects of motif-specific blockade on substrate recognition, ubiquitin ligase activity, or complex assembly. Such experiments advance the understanding of critical regulatory elements within the cell division machinery.

Structural and biophysical characterization: The availability of the CDC27 (760-771) peptide supports structural analyses such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), or crystallography, providing atomic-level insight into the conformational properties of the C-terminal motif. These studies inform on the secondary structure, flexibility, and potential interaction surfaces of the peptide, contributing to broader efforts to model APC/C architecture and dynamics. By integrating structural data with functional assays, researchers gain a comprehensive perspective on the role of CDC27's C-terminal region in cell cycle regulation.

Source#
Homo sapiens (human)
Epitope
760-771
Restricting HLA
HLA-DR4
References
Wang; Science 1999

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