MBD3 (H250) pAb

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Catalogue No : BS2250

Alternative Name for MBD3 (H250) pAb
Host   Reactivity Size Application stock price cart
Rabbit H,M 100μg WB 258.00
Contact information

Email:shdiahds@163.com
Phone:+1-909-839-7620
Fax:+1-909-839-7620

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Product

1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.

Molecular Weight

~ 33 kDa

Purification & Purity

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Specificity

MBD3 (H250) pAb detects endogenous levels of MBD3 protein.

Applications (Recommended Dilutions)

WB: 1:500~1:1000

Western Blot(WB)

Western blot (WB) analysis of MBD3 (H250) pAb in extracts from Jurkat cells.

Storage&Stability

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Background

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) (Bhattacharya et al.). 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 (Hendrich et al.). 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 has homology to bacterial base excision repair DNA N-glycosylases/lyases (Petronzelli et al.). In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract (Bader et al.).