|Detection of Human RNF8 by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line and U2OS human osteosarcoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human RNF8 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7114) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for RNF8 at approximately 65 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
RNF8 (RING [really interesting gene] finger protein 8; also E3 ubiquitin-protein ligase RNF8) is a 55-58 kDa member of the RNF8 family of proteins. It is ubiquitously expressed, and serves as an E3 ubiquitin ligase. RNF8 is recruited to DNA double-strand breaks by phosphoMDC1, where it promotes the ubiquitination of histones H2A and H2AX. This, in turn, may result in the recruitment of 53BP1, a scaffold protein that holds DNA damage response elements. Human RNF8 is 485 amino acids (aa) in length. It contains one forkhead associated domain (aa 38-92), a Gln-rich segment (aa 276-345), and one Zn-finger region (aa 403-441). There is one utilized phosphorylation site at Ser157. Two potential isoforms are reported. One shows an 18 aa substitution for aa 81-485, while another possesses a 36 aa substitution for aa 413-485. RNF8 apparently undergoes ubiquitination, generating multiple isoforms that run at 62-72 kDa in SDS-Page. Over aa 1-124, human RNF8 shares 74% aa identity with mouse RNF8.
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