Anti-MBD4 antibody produced in rabbit

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.

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.

Anti-MBD4 antibody produced in rabbit has been used in immunoblotting and chromatin-immunoprecipitation (ChIP).

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.

Solution in 0.01 M phosphate buffered saline containing 1% bovine serum albumin (BSA) and 15 mM sodium azide.

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