| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| FC | 1:50-1:200 |
MBD2 (Methyl-CpG-binding domain protein 2) plays a central role in epigenetic gene regulation by recognizing and binding methylated CpG dinucleotides in genomic DNA. As a core component of the NuRD chromatin remodeling complex, MBD2 functions as a transcriptional repressor that interprets DNA methylation patterns to silence gene expression. This positions MBD2 at the intersection of epigenetic research, cancer biology, and developmental studies, where aberrant DNA methylation patterns frequently contribute to disease pathogenesis.
This recombinant monoclonal antibody (clone 3E5) offers the reproducibility essential for epigenetic research, where subtle changes in protein expression can carry significant biological meaning. Generated in rabbit against a synthetic peptide derived from human MBD2, the recombinant format ensures sequence-defined consistency across experiments and eliminates the lot-to-lot variability that can complicate longitudinal studies or multi-site collaborations.
Validation studies confirm reliable performance across multiple platforms. In western blot applications, the antibody detects MBD2 in HEK293 whole cell lysates at dilutions of 1:500–1:2000, with an observed band at 29 kDa. The 29 kDa band detected by this recombinant anti-MBD2 antibody in HEK293 lysates corresponds to the endogenously processed, mature form of MBD2 resulting from N-terminal cleavage (or alternative splicing), which migrates faster than the predicted 43 kDa full-length precursor against which the immunizing synthetic peptide was designed. Flow cytometry validation in Raji cells demonstrates clear separation from isotype controls at 1:50–1:200 dilutions, enabling intracellular detection of MBD2 in lymphoid cell populations.
This antibody supports investigations into DNA methylation-mediated gene silencing, chromatin remodeling mechanisms, and the epigenetic alterations underlying cancer progression and cellular differentiation.
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