Anti-Human RNF168 Antibody Pair

Product Description: Ring finger protein 168 (RNF168) is a RING-type E3 ubiquitin ligase characterized by a core RING finger domain with a unique bent central alpha-helix, distinguishing it structurally from related proteins such as TRAF6, CHIP, and RNF8. RNF168 plays a crucial role in the DNA damage response, particularly in the repair of double-strand breaks (DSBs). Upon DNA damage, RNF168 is recruited to chromatin at DSB sites in an MDC1-dependent manner, where it ubiquitinates histones H2A and H2AX, thereby amplifying the DNA damage signal and facilitating the recruitment of downstream repair factors such as BRCA1 and 53BP1. This ubiquitination is essential for maintaining genome stability. Mutations in RNF168 are associated with RIDDLE syndrome, a rare disorder characterized by radiosensitivity, immunodeficiency, dysmorphic features, and learning difficulties. Protein Function: E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro, possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively) [The Uniprot Consortium]