Anti-MBD4/MED1 Antibody Picoband® Fluoro594 Conjugated

Methyl-CpG-binding domain protein 4 is a protein that in humans is encoded by the MBD4 gene. It is mapped to 3q21.3. The protein encoded by this gene is a member of a family of nuclear proteins related by the presence of a methyl-CpG binding domain (MBD) . These proteins are capable of binding specifically to methylated DNA, and some members can also repress transcription from methylated gene promoters. This protein contains an MBD domain at the N-terminus that functions both in binding to methylated DNA and in protein interactions and a C-terminal mismatch-specific glycosylase domain that is involved in DNA repair. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.

Methyl-CpG-binding domain protein 4; Methyl-CpG-binding endonuclease 1; Methyl-CpG-binding protein MBD4; Mismatch-specific DNA N-glycosylase; MBD4; MED1

Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.

1. Hendrich, B., Abbott, C., McQueen, H., Chambers, D., Cross, S., Bird, A. Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes. Mammalian Genome 10: 906-912, 1999. 2. Hendrich, B., Bird, A. Identification and characterization of a family of mammalian methyl-CpG binding proteins. Molec. Cell. Biol. 18: 6538-6547, 1998. 3. Hendrich, B., Hardeland, U., Ng, H.-H., Jiricny, J., Bird, A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 401: 301-304, 1999. Note: Erratum: Nature 404: 525 only, 2000.