Human MBD4 protein encodes an alternative spliced form which lacks C-terminal 42 amino acids.
Methyl-CpG binding domain protein 4 (MBD4) is a thymine glycosylase which possesses a carboxy-terminal DNA glycosylase domain and an amino-terminal MBD domain. It belongs to the methyl-CpG-binding protein family.
Immunogen
synthetic peptide corresponding to amino acids 541-554 of mouse MBD4 conjugated to KLH via an N-terminal added cysteine residue. The sequence is conserved in human.
Application
Anti-MBD4 antibody produced in rabbit has been used in immunoblotting and chromatin-immunoprecipitation (ChIP).
Biochem/physiol Actions
Methyl-CpG binding domain protein 4 (MBD4) plays an important role in DNA demethylation. It can remove mismatched bases which are present with a guanine. The preferred substrate for MBD4 is thymine over N4-ethenocytosine.
The methyl-CpG binding domain of MBD4 binds preferentially to 5-methylcytosine CpG-TpG mismatches, the primary product of deamination at methyl-CpG. The combined specificities of binding and catalysis indicates that this protein may function to minimize mutation at methylCpG. in vivo, the DNA repair properties of MBD4 suggests that it plays a role in suppressing mutability and tumorigenesis.
Physical form
Solution in 0.01 M phosphate buffered saline containing 1% bovine serum albumin (BSA) and 15 mM sodium azide.
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The mammalian DNA glycosylase--methyl-CpG binding domain protein 4 (MBD4)--is involved in active DNA demethylation via the base excision repair pathway. MBD4 contains an N-terminal MBD and a C-terminal DNA glycosylase domain. MBD4 can excise the mismatched base paired with a
Oxidative stress induces genome-wide remodeling of the chromatin structure. In this study, we identify Methyl-CpG Binding Protein 4 (MBD4), a multifunctional enzyme involved in DNA demethylation, base excision repair, and gene expression regulation, as an essential factor in response to
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