Anti-MBD2 + MBD3 monoclonal antibody, clone 217C702

Antibody Isotype

IgG1

Clone

217C702

Species Reactivity

Human

Immunogen

Synthetic peptide: CKAFMVTDEDIRKQEE, corresponding to amino acids 215-230 of Human MBD3

Conjugate

Application Notes

ICC/IF: 1/400; WB: 2 μg/ml; Flow Cyt: 1μg/10⁶ cells.

Alternative Names

Demethylase; DMTase; MBD 2; MBD 3; Methyl CpG binding domain protein 2; Methyl CpG binding domain protein 3; Methyl CpG binding protein MBD2; Methyl CpG binding protein MBD3; MBD2 + MBD3

Entrez Gene ID

Antigen Description

DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.