ARID3A (F1G2E) Rabbit Monoclonal Antibody #43033

AT-rich interactive domain-containing protein 3A (ARID3A), also known as B-cell regulator of IgH transcription (Bright), is a multifaceted DNA-binding protein and a member of the extensive ARID family of proteins, many of which are recognized for their roles in chromatin remodeling and epigenetic regulation. ARID3A contains an ARID domain, a conserved DNA-binding motif that allows for recognition and binding to AT-rich DNA sequences (1). This protein typically functions as a dimer (and can form heterodimers with ARID3B) for its DNA-binding activity (2,3). Beyond binding to DNA, ARID3A is also involved in chromatin remodeling and can influence chromatin accessibility. For instance, in the context of immunoglobulin (Ig) gene regulation, it has been shown to increase the accessibility of the Ig heavy chain enhancer (4). ARID3A has been shown to play an essential role in embryonic development and hematopoiesis as ARID3A knockout mice exhibit early embryonic lethality due to severe defects in both early hematopoietic stem cell populations and erythropoiesis (5,6). ARID3A has also been linked to autoimmune diseases, particularly systemic lupus erythematosus (SLE), where increased ARID3A expression in B cells and other hematopoietic cell types correlates with increased disease severity (7). Moreover, ARID3A misregulation is also implicated in various cancers (8-10).

Importantly, various post-translational modifications such as phosphorylation, ubiquitination, and SUMOylation on ARID3A have been identified, and SUMOylation of this protein specifically underscores a key mechanism for targeting and modulating its transcriptional activity (11).