MBD4 (methyl-CpG binding domain 4, DNA glycosylase) is a methyl-CpG-binding endonuclease. It is a tripartite with an N-terminal 5-methylcytosine binding domain (MBD), a C-terminal catalytic domain with homology to bacterial DNA damage-specific glycosylases/lyases and a core region with five putative nuclear localization signals.
Synonyms: Anti-Methyl-CpG-binding domain protein 4 antibody produced in rabbit; Anti-Methyl-CpG-binding endonuclease 1 antibody produced in rabbit; Anti-Methyl-CpG-binding protein MBD4 antibody produced in rabbit; Anti-Mismatch-specific DNA N-glycosylase antibody produced in rabbit
MDL Number: MFCD05665239
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: MBD4 (methyl-CpG binding domain 4, DNA glycosylase) is involved in the maintenance of genomic integrity. It acts as a DNA repair protein in the DNA mismatch repair (MMR) system. During DNA repair, MBD4 couples with MMR protein MLH1 (mutL homolog 1) that binds to the methyl-CpG-containing DNA to perform endonuclease activity. MBD4 also has impact on glycosylase/lyase activity in a pathway of base excision repair. It has been reported that mutation in MED1 activity may cause irregular DNA damage and tumor development.
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