cell division cycle 45-like (556-564)

Cell division cycle 45-like (556-564) is a synthetic peptide fragment derived from the CDC45 protein, a key component involved in the initiation and progression of DNA replication within eukaryotic cells. As a segment corresponding to amino acids 556 through 564 of the CDC45 sequence, this peptide provides a valuable molecular tool for dissecting the mechanistic roles of CDC45 in cell cycle regulation and DNA synthesis. The unique sequence and structural properties of this peptide enable its use in a range of experimental applications, supporting research on protein-protein interactions, post-translational modifications, and the functional mapping of replication complexes. Its relevance is underscored by the centrality of CDC45 to the assembly and activation of the replicative helicase machinery, making this peptide fragment a significant resource for molecular and cellular biology investigations.

Peptide mapping: The 556-564 fragment is frequently utilized in peptide mapping studies aimed at identifying functional domains within the CDC45 protein. By employing this synthetic peptide in binding assays or structural analyses, researchers can delineate the specific contributions of this region to the assembly and activity of the CMG (Cdc45-MCM-GINS) helicase complex. Such mapping efforts facilitate the understanding of how CDC45 coordinates with other replication factors during the initiation of DNA synthesis, providing insights into the spatial organization and regulatory checkpoints of the DNA replication machinery.

Antibody production: As an antigenic epitope, the CDC45-like (556-564) peptide is well-suited for generating sequence-specific antibodies. Immunization protocols utilizing this defined peptide sequence enable the production of polyclonal or monoclonal antibodies that selectively recognize the corresponding region of the full-length CDC45 protein. These antibodies are invaluable for applications such as immunoblotting, immunoprecipitation, and immunofluorescence, where precise detection of CDC45 is required to track its localization, expression dynamics, or interaction networks during the cell cycle.

Protein interaction studies: The peptide serves as a model substrate for investigating protein-protein interactions involving the C-terminal region of CDC45. By incorporating the 556-564 sequence into affinity assays, surface plasmon resonance experiments, or peptide pull-down protocols, researchers can screen for binding partners or regulatory factors that associate with this domain. Such studies are critical for elucidating how CDC45 interfaces with other cell cycle regulators, replication origins, or checkpoint proteins, thereby advancing the molecular understanding of cell cycle control.

Phosphorylation analysis: The defined sequence of the CDC45-like (556-564) peptide allows for targeted studies on post-translational modifications, particularly phosphorylation events that may regulate CDC45 function. In vitro kinase assays employing this peptide can identify potential phosphorylation sites, characterize kinase-substrate specificity, and assess the impact of phosphorylation on peptide conformation or binding properties. These analyses contribute to a broader comprehension of how CDC45 activity is modulated in response to cell cycle cues and DNA damage signals.

Assay development: The synthetic peptide fragment is an effective standard or control in the development and optimization of analytical assays targeting CDC45 or related replication factors. By providing a consistent and well-characterized peptide standard, it supports the calibration of mass spectrometry workflows, validation of immunoassays, and benchmarking of peptide quantification methods. This enhances assay reliability and reproducibility, which are essential for high-throughput screening, proteomic profiling, and functional genomics studies centered on cell cycle regulation and DNA replication fidelity.

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