UV excision repair protein RAD23 homolog B isoform 2 (268-281)

UV excision repair protein RAD23 homolog B isoform 2 (268-281) is a synthetic peptide fragment derived from the human RAD23B protein, specifically corresponding to amino acid residues 268 through 281 of isoform 2. As a segment of a protein integral to the nucleotide excision repair (NER) pathway, this peptide represents a valuable molecular tool for investigating DNA damage recognition and repair mechanisms. The functional region encoded by this sequence is implicated in protein-protein interactions and post-translational modification events essential for cellular responses to genotoxic stress, making it highly relevant in studies of genome stability and cellular defense systems.

Protein-protein interaction studies: The peptide serves as a precise probe for dissecting the molecular interactions involving the C-terminal region of RAD23B isoform 2. By employing this fragment in in vitro binding assays, researchers can map interaction motifs, identify novel binding partners, and characterize affinity changes resulting from sequence modifications or post-translational modifications. Such studies are fundamental in elucidating the assembly and regulation of multiprotein complexes involved in DNA repair pathways.

Antibody epitope mapping: Due to its defined sequence and structural relevance, the RAD23B (268-281) peptide is frequently utilized as an antigen in the generation and validation of antibodies specific to the corresponding region of the native protein. This application is critical for developing high-specificity reagents for immunodetection techniques, enabling precise localization and quantification of RAD23B isoform 2 in cellular and tissue samples, and facilitating studies of protein expression dynamics under various stress conditions.

Phosphorylation and post-translational modification analysis: The sequence encompassed by this peptide includes potential sites for phosphorylation or other regulatory modifications. Synthetic versions of the fragment allow for controlled in vitro assays to investigate how such modifications influence RAD23B function, stability, or interactions. These studies contribute to a deeper understanding of post-translational regulatory mechanisms governing DNA repair factors and their response to UV-induced damage.

Structural and conformational studies: The defined length and sequence of the peptide make it suitable for biophysical analyses, such as circular dichroism, NMR spectroscopy, or crystallography, aimed at elucidating local secondary structure or conformational changes upon binding to other biomolecules. Insights gained from these studies can inform the design of inhibitors, mimetics, or modified peptides for research applications focused on modulating DNA repair processes.

Synthetic peptide control and assay development: The RAD23B (268-281) fragment functions as a reliable positive control or standard in a variety of biochemical assays, including mass spectrometry-based peptide quantification, ELISA, and peptide array platforms. Its use ensures assay reproducibility and specificity, supporting the development and validation of robust analytical methods for DNA repair research and related fields.

1. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function

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

4. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I

5. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review