RAD23D Antibody

Structure and Functional Domains

RAD23D, like other RAD23 proteins, contains:

• N-terminal ubiquitin-like (UBL) domain: Facilitates interaction with the 26S proteasome via RPN10.

• Rad4/XPC-binding domain: Stabilizes DNA damage recognition in NER.

• C-terminal ubiquitin-associated (UBA) domains: Bind polyubiquitin chains to target substrates for degradation.

Role in Nucleotide Excision Repair (NER)

RAD23D contributes to global genomic NER by:

• Stabilizing XPC (Rad4 in yeast): Enhances DNA damage binding and repair efficiency .

• Complementing repair defects: Partial repair activity in rad23 mutants requires Rad23 and Rad4 synergy .

Proteasome-Mediated Degradation

RAD23D acts as a ubiquitin receptor:

• Binds 'Lys-48'-linked polyubiquitin chains: Prefers multiubiquitin tags over single chains .

• Interacts with RPN10: Facilitates substrate delivery to the 26S proteasome .

Stress Response and Protein Homeostasis

• Drought tolerance in plants: MdRAD23D1 (apple homolog) interacts with MdPRP6 to modulate stress-induced proteolysis .

• Neurodegeneration models: RAD23 knockdown accelerates degradation of toxic proteins (e.g., mutSOD1, mutTDP-43) in ALS models .

Available RAD23D Antibodies and Reagents

While RAD23D-specific antibodies are scarce, polyclonal antibodies targeting the RAD23 family (A-D) are available:

Note: RAD23D-specific antibodies are not explicitly listed in current databases. Researchers often use cross-reactive antibodies validated for broader RAD23 family detection.

Western Blotting

• Plant studies: Use anti-RAD23A-D antibodies to monitor protein abundance in Arabidopsis under stress .

• Human studies: RAD23B-specific antibodies (e.g., BioLegend #8355) distinguish isoforms in proteasome research .

Immunoprecipitation

• Protein interaction assays: Co-IP RAD23D with RPN10 or XPC to study repair complex assembly .

Subcellular Localization

• Immunofluorescence: RAD23 proteins localize to the nucleus and cytoplasm, with cell cycle-dependent dynamics .

Key Research Challenges

1. Isoform specificity: Most antibodies target conserved regions, limiting RAD23D-specific detection.

2. Functional redundancy: Overlapping roles among RAD23A-D complicate isoform-specific analysis.

3. Species variation: Plant (e.g., Arabidopsis, apple) and human RAD23 homologs diverge in subcellular localization and stress responses .

Future Directions

• Development of RAD23D-specific antibodies: Critical for elucidating isoform-specific roles in NER and stress adaptation.

• Structural studies: Cryo-EM or X-ray crystallography to map RAD23D-ubiquitin/proteasome interactions.

• Therapeutic targeting: Exploiting RAD23D’s role in proteostasis for neurodegenerative or stress-related diseases .