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MBD3 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - MBD3 Antibody (C-term) AP1038c
    Western blot analysis of MBD3 (arrow) using rabbit polyclonal MBD3 Antibody (C-term) (Cat.#AP1038c).293 cell lysates (2 ug/lane) either nontransfected (Lane 1) or transiently transfected with the MBD3 gene (Lane 2) (Origene Technologies).
  • 14 - MBD3 Antibody (C-term) AP1038c
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, E
Primary Accession O95983
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 32844 Da
Additional info
Gene ID 53615
Other Names Methyl-CpG-binding domain protein 3, Methyl-CpG-binding protein MBD3, MBD3
Target/Specificity This MBD3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 264-291 amino acids from the C-terminal region of human MBD3.
Dilution WB~~1:1000
IHC-P~~1:50~100
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMBD3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name MBD3
Function Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to DNA by itself (PubMed:12124384). Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases.
Cellular Location Nucleus. Chromosome. Note=Nuclear, in discrete foci. Detected on chromatin, at promoter regions of active genes
Research Areas

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). 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.

REFERENCES

Bhattacharya SK, Ramchandani S, Cervoni N, Szyf. M. Nature, 397 (6720):579-583 1999.
Hendrich B and Bird A. Mol Cell Biol, 18: 6538-6547(1998).
Petronzelli F, Riccio A, Markham GD, Seeholzer SH, Stoerker J, Genuardi M, Yeung AT, Matsumoto Y, Bellacosa A. J Biol Chem 275 (42): 32422-32429 (2000).
Bader S, Walker M, Harrison D. Br J Cancer 83(12): 1646-1649 (2000).

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