G1/S-specific cyclin-D1 (198-212)

G1/S-specific cyclin-D1

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

CAT No: ta-319

Synonyms/Alias:G1/S-specific cyclin-D1 (198-212)

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cGMP Peptide
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  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
Sequence
NPPSMVAAGSVVAAV
Areas of Interest
Antigen-presenting Cells; Cancer Research

G1/S-specific cyclin-D1 (198-212) is a synthetic peptide fragment corresponding to amino acids 198 through 212 of the human cyclin D1 protein, a key regulator of cell cycle progression at the G1/S transition. As a segment of the cyclin D1 protein, this peptide encompasses a region implicated in protein-protein interactions and regulatory phosphorylation events that modulate cyclin-dependent kinase (CDK) activity. Its defined sequence and structural features make it a valuable tool for researchers investigating the molecular mechanisms of cell cycle control, protein signaling networks, and post-translational modifications within the cyclin D family. The availability of this peptide enables targeted experimental approaches in both basic and applied bioscience contexts, supporting the elucidation of cyclin D1's role in cellular proliferation and checkpoint regulation.

Cell cycle research: The peptide fragment representing residues 198-212 of cyclin D1 provides a precise molecular probe for dissecting the regulatory events at the G1/S transition. By employing this peptide in in vitro assays, researchers can investigate how this specific region contributes to cyclin D1's interactions with CDKs and other cell cycle regulators. Such studies are instrumental in mapping the structural determinants of cell cycle progression and identifying potential sites of regulatory phosphorylation or ubiquitination that influence protein stability and function.

Protein interaction studies: As a discrete segment of cyclin D1, the 198-212 peptide can be utilized in binding assays to characterize interactions with known or novel cyclin partners. Pull-down assays, surface plasmon resonance, or fluorescence polarization techniques employing this peptide facilitate the identification and quantification of binding affinities between cyclin D1 and its interacting proteins. These experiments help delineate the molecular basis of cyclin D1-mediated signaling pathways and may reveal new regulatory nodes within the cell cycle machinery.

Antibody production and validation: The defined sequence of the cyclin D1 (198-212) peptide serves as an effective immunogen for the generation of sequence-specific antibodies. Polyclonal or monoclonal antibodies raised against this fragment can be used to detect the native cyclin D1 protein or its processed forms in various biological samples. Furthermore, the peptide is valuable in antibody validation protocols, such as peptide competition assays, ensuring antibody specificity and supporting high-confidence immunodetection in western blotting, immunoprecipitation, or immunohistochemistry applications.

Phosphorylation and post-translational modification analysis: The 198-212 region of cyclin D1 is a target for regulatory phosphorylation events that can modulate its activity or subcellular localization. Synthetic peptides corresponding to this region allow for in vitro kinase assays to assess the substrate specificity of candidate kinases or to map phosphorylation sites by mass spectrometry. This approach aids in deciphering the functional consequences of post-translational modifications on cyclin D1 and provides insight into the dynamic regulation of cell cycle checkpoints.

Epitope mapping and structural studies: The peptide fragment can be employed in epitope mapping experiments to identify antibody binding sites or to probe conformational epitopes within the full-length cyclin D1 protein. Additionally, its defined structure is suitable for use in biophysical studies, such as nuclear magnetic resonance (NMR) or crystallography, to investigate local folding, secondary structure propensity, or peptide-macromolecule interactions. These applications contribute to a detailed understanding of cyclin D1's structural and functional landscape, advancing research in cell cycle biology and protein engineering.

Source#
Homo sapiens (human)
Epitope
198-212
Restricting HLA
HLA-DR4
References
Dengjel; Eur J Immunol 2004

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