WB-Western Blot IP-Immunoprecipitation IHC-Immunohistochemistry IF-Immunofluorescence ICC-Immunocytochemistry FC-Flow Cytometry

Rad23A  also designated HR23A is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair. Rad23A plays a critical role in nucleotide excision repair (NER), a vital cellular mechanism that removes DNA lesions caused by ultraviolet light and other forms of damage. Rad23A protein is essential for maintaining genomic stability, as Rad23A helps ensure damaged DNA is accurately repaired, thereby preventing mutations that could lead to cancer and other diseases. Rad23A protein interacts with the 26S proteasome, facilitating the degradation of damaged proteins and contributing to cellular homeostasis. Rad23A protein′s structure includes an N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain, both of which are crucial for function and are conserved across species from yeast to humans. These domains allow Rad23A protein to effectively mediate repair processes and regulate proteasome activity, highlighting Rad23A′s importance in cellular responses to DNA damage.