Anti-MBD1 (Clone: ABM15H2)

MBD1 (Methyl-CpG-Binding Domain Protein 1) protein is a primary candidate for the readout of DNA methylation as it recruits chromatin remodelers, histone deacetylases and methylases to methylated DNA associated with gene repression. This protein, a member of a transcriptional repressor family MBD, is predominantly expressed in neurons. MBD protein binding requires both functional MBD domains and methyl-CpGs, however, some MBD proteins also bind unmethylated DNA and active regulatory regions via alternative regulatory domains or interaction with the NuRD/Mi-2 (Nucleosome Remodeling Deacetylase) complex members. The CXXC3 domain of MBD1 makes it a unique member of the MBD family due to its affinity to unmethylated DNA. MBD1 acts as an epigenetic regulator via different mechanisms, such as the formation of the MCAF1/MBD1/SETDB1 complex or the MBD1-HDAC3 complex. It also plays an important role in disease progression, contributes to the drug resistance of PC cells, however, the mechanism underlying the drug resistance endowed by MBD1 remains unknown. Protein function: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters. [The UniProt Consortium]