Topoisomerase II-alpha-b (828-836)

Topoisomerase II-alpha-b (828-836) is a synthetic peptide fragment derived from the C-terminal region of the human DNA topoisomerase II alpha enzyme. As a peptide corresponding to amino acid residues 828 to 836, it represents a specific sequence within a critical domain of this essential nuclear enzyme, which plays a central role in DNA replication, transcription, and chromosome segregation. Topoisomerase II alpha is a well-characterized target in cell cycle regulation and genomic stability research, making this peptide fragment a valuable tool for investigating protein-protein interactions, post-translational modifications, and the structural determinants of enzyme function. Its defined sequence and biochemical relevance position it as a versatile reagent for a range of molecular and cellular biology applications.

Epitope mapping: The Topoisomerase II-alpha-b (828-836) peptide is frequently utilized in epitope mapping studies, particularly for characterizing antibody specificity against topoisomerase II alpha. By providing a defined linear epitope, the peptide enables researchers to identify and validate antibody binding sites, facilitating the development of highly specific immunodetection reagents. Such applications are critical for refining immunoassays, optimizing western blot protocols, and improving the accuracy of immunoprecipitation experiments involving topoisomerase II alpha.

Protein interaction studies: As a segment of the topoisomerase II alpha protein, this peptide serves as a functional probe for investigating protein-protein interactions that involve the 828-836 region. Researchers can employ it in pull-down assays, surface plasmon resonance, or other biophysical techniques to elucidate binding partners and interaction domains. These studies provide valuable insights into the regulatory mechanisms and cofactor associations that modulate topoisomerase II alpha activity within the cellular context.

Phosphorylation and post-translational modification analysis: The sequence encompassed by this peptide includes potential sites for phosphorylation and other post-translational modifications. Synthetic peptides like Topoisomerase II-alpha-b (828-836) are widely used as substrates in kinase assays or as standards in mass spectrometry-based proteomics to assess modification patterns. Such applications are instrumental in dissecting the regulation of topoisomerase II alpha by cell cycle-dependent kinases or other modifying enzymes, thereby advancing understanding of enzyme control and signal transduction pathways.

Peptide-based inhibitor screening: The defined structure of this peptide fragment allows it to be employed in screening assays to identify small molecules or biologics that disrupt interactions involving the 828-836 region. By serving as a competitive substrate or binding partner, the peptide facilitates the discovery and characterization of inhibitors that target specific functional motifs within topoisomerase II alpha. These studies are relevant for the development of molecular probes or research tools aimed at modulating enzyme function in vitro.

Immunogen for antibody production: Owing to its unique sequence, the Topoisomerase II-alpha-b (828-836) peptide can be conjugated to carrier proteins and used as an immunogen to generate sequence-specific polyclonal or monoclonal antibodies. These custom antibodies offer enhanced specificity for the targeted region of topoisomerase II alpha, supporting advanced research applications such as chromatin immunoprecipitation, immunofluorescence, and quantitative immunoassays. The use of such peptide immunogens is fundamental for producing reagents tailored to precise scientific requirements in molecular and cellular biology.

1. Effect of Probiotic Lactobacillus plantarum on Streptococcus mutans and Candida albicans Clinical Isolates from Children with Early Childhood Caries

2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

3. GLP-1, exendin-4 and C-peptide regulate pancreatic islet microcirculation, insulin secretion and glucose tolerance in rats

4. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate

5. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle