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FIGURE: 1 / 8
MBD4 Antibody (PA5-115552) in ICC/IF
Immunocytochemistry analysis of MBD4 in HepG2 cells. Samples were treated with PFA, permeabilized in 0.1% Triton X-100, blocked in 10% serum (45 min at 25°C), and incubated with polyclonal antibody (Product # PA5-115552). Secondary staining was applied with mouse anti-beta tubulin (1 hr at 37°, AlexaFluor 594 conjugated goat anti-rabbit IgG (Red), AlexaFluor 488 conjugated goat anti-mouse IgG (Green) and DAPI.
Product Details
PA5-115552
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human,
Mouse,
Rat
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
A synthesized peptide derived from human MBD4(Accession O95243), corresponding to amino acid residues S318-K368.
Conjugate
Form
Liquid
Concentration
1 mg/mL
Purification
Affinity chromatography
Storage buffer
PBS with 50% glycerol
Contains
0.02% sodium azide
Storage conditions
-20°C
Shipping conditions
Wet ice
RRID
AB_2900188
Product Specific Information
Antibody detects endogenous levels of total MBD4.
Target Information
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: 3,N(4)-ethenocytosine glycosylase; G/5-fluorouracil mismatch glycosylase with biphasic kinetics; G/T mismatch glycosylase; G/U mismatch glycosylase; methyl-CpG binding domain 4 DNA glycosylase; methyl-CpG binding domain protein 4; Methyl-CpG-binding domain protein 4; Methyl-CpG-binding endonuclease 1; Methyl-CpG-binding protein MBD4; Mismatch-specific DNA N-glycosylase; putative methyl-CpG binding protein
Gene Aliases: MBD4; MED1
UniProt ID: (Human) O95243, (Mouse) Q9Z2D7
Entrez Gene ID: (Human) 8930, (Mouse) 17193, (Rat) 680915
satellite DNA binding
endodeoxyribonuclease activity
protein binding
pyrimidine-specific mismatch base pair DNA N-glycosylase activity
DNA N-glycosylase activity
purine-specific mismatch base pair DNA N-glycosylase activity
DNA binding
catalytic activity
uracil DNA N-glycosylase activity
hydrolase activity
single-strand selective uracil DNA N-glycosylase activity
DNA-3-methylbase glycosylase activity
nicotinamide riboside hydrolase activity
nicotinic acid riboside hydrolase activity
deoxyribonucleoside 5'-monophosphate N-glycosidase activity
molecular_function
DNA metabolism protein
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