Rad23B Antibody (F-8): sc-390019

Rad23B Antibody (F-8) is a mouse monoclonal IgG1 antibody that detects Rad23B in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Rad23B plays a critical role in the nucleotide excision repair (NER) pathway, which is essential for maintaining genomic stability by repairing UV-induced DNA damage. Rad23B is predominantly located in the nucleus, where Rad23B interacts with the 26S proteasome, facilitating the degradation of damaged proteins and thus preventing the accumulation of potentially harmful cellular components. Rad23B (F-8) antibody helps detect a protein vital for the stability of the xeroderma pigmentosum C protein (XPC), as Rad23B absence significantly reduces XPC levels, highlighting its importance in DNA repair mechanisms. Additionally, anti-Rad23B antibody (F-8) recognizes a conserved ubiquitin-like domain that is crucial for biological functions, underscoring its evolutionary significance from yeast to humans. Rad23B monoclonal antibody (F-8) serves as an invaluable tool for researchers studying DNA repair processes and cellular response to genotoxic stress, providing insights into molecular mechanisms underlying various diseases, including cancer.

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Rad23B Antibody (F-8) References:

1. Expression of a novel RAD23B mRNA splice variant in the human testis.  |  Huang, X., et al. 2004. J Androl. 25: 363-8. PMID: 15064313
2. Epigenetic silencing of the human nucleotide excision repair gene, hHR23B, in interleukin-6-responsive multiple myeloma KAS-6/1 cells.  |  Peng, B., et al. 2005. J Biol Chem. 280: 4182-7. PMID: 15550378
3. Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B.  |  Kim, B., et al. 2005. FEBS J. 272: 2467-76. PMID: 15885096
4. Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct.  |  Neher, TM., et al. 2010. Biochemistry. 49: 669-78. PMID: 20028083
5. Genetic polymorphisms in RAD23B and XPC modulate DNA repair capacity and breast cancer risk in Puerto Rican women.  |  Pérez-Mayoral, J., et al. 2013. Mol Carcinog. 52 Suppl 1: E127-38. PMID: 23776089
6. Erythropoietic defect associated with reduced cell proliferation in mice lacking the 26S proteasome shuttling factor Rad23b.  |  Bergink, S., et al. 2013. Mol Cell Biol. 33: 3879-92. PMID: 23897431
7. Interaction of Nucleotide Excision Repair Protein XPC-RAD23B with DNA Containing Benzo[a]pyrene-Derived Adduct and Apurinic/Apyrimidinic Site within a Cluster.  |  Starostenko, LV., et al. 2016. Biochemistry (Mosc). 81: 233-41. PMID: 27262192
8. Circular RNA circ-RAD23B promotes cell growth and invasion by miR-593-3p/CCND2 and miR-653-5p/TIAM1 pathways in non-small cell lung cancer.  |  Han, W., et al. 2019. Biochem Biophys Res Commun. 510: 462-466. PMID: 30722989
9. Irisin attenuates lipopolysaccharide-induced acute lung injury by downregulating inflammatory cytokine expression through miR-199a-mediated Rad23b overexpression.  |  Ma, LY., et al. 2021. Exp Cell Res. 404: 112593. PMID: 33961841
10. RAD23B mediated proteasomal degradation occurs through p38 MAPK/ATF-2/RAD23B axis under nutrient-deprived conditions in breast cancer.  |  Sriaishwarya, S. and Lakshmi, BS. 2024. Cell Biol Int.. PMID: 38561940

The preferred Rad23B antibody is Rad23B Antibody (H-8): sc-137088.