HMGN1 (D1I5O) Rabbit mAb #12734

High mobility group (HMG) proteins are a superfamily of abundant and ubiquitous nuclear proteins that bind DNA without sequence specificity and induce structural changes to the chromatin fiber to regulate access to the underlying DNA. The HMGN family of proteins, which includes five members (HMGN1-5), is characterized by the presence of several conserved protein domains: a positively charged domain, a nucleosome binding domain, and an acidic C-terminal chromatin-unfolding domain (1,2). HMGN proteins function in transcriptional regulation and are recruited to gene promoters by transcription factors, such as estrogen receptor α (ERα), serum responsive factor (SRF), and PITX2, where they can facilitate either gene activation or repression (3-5). HMGN proteins bind specifically to nucleosomal DNA and reduce compaction of the chromatin fiber, in part by competing with linker histone H1 for nucleosome binding (6). In addition, HMGN proteins act to modulate local levels of post-translational histone modifications, decreasing phosphorylation of histone H3 at Ser10 and histone H2A at Ser1 and increasing acetylation of histone H3 at Lys14 (7-9). HMGN proteins can also modulate the activity of several chromatin-remodeling factors and restrict nucleosome mobility (10).