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Validated All-in-One™ qPCR Primer for DNMT3L(NM_175867.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a nuclear protein with similarity to DNA methyltransferases. This protein is not thought to function as a DNA methyltransferase as it does not contain the amino acid residues necessary for methyltransferase activity. However, this protein does stimulate de novo methylation by DNA cytosine methyltransferase 3 alpha and it is thought to be required for the establishment of maternal genomic imprints. This protein also mediates transcriptional repression through interaction with histone deacetylase 1. Alternative splicing results in two transcript variants. An additional splice variant has been described but its biological validity has not been determined.
Gene References into function
- DNMT3L stimulates de novo methylation by Dnmt3a.
- The carboxyl-terminal half of DNMT3L was found to be responsible for the stimulation of the DNA methylation activity of Dnmt3a and Dnmt3b.
- Regulates germ cell-specific gene expression and intracisternal A-particle suppression, which are critical for male germ cell proliferation and meiosis.
- Dnmt3L-Dnmt3b interactions play an important role in the regulation of DNA methylation during mammalian development.
- The acquisition of DNMT3L by a common ancestor of eutherians and marsupials might have been closely related to the evolution of imprinting.
- Data show that binding of DNMT3L to DNMT3A2 promotes reorganization of DNMT3A2 subunits and leads to formation of specific complexes with enhanced DNA methyltransferase activity and increased S-adenosyl-L-methionine binding.
- Crystallographic studies of human DNMT3L showed that the protein has a carboxy-terminal methyltransferase-like domain and an N-terminal cysteine-rich domain
- the carboxy-terminal domain of human Dnmt3L interacts with the catalytic domain of Dnmt3a, demonstrating that Dnmt3L has dual functions of binding the unmethylated histone tail and activating DNA methyltransferase
- Importance of DNA methylation profile at DNMT3L promoter not only as a promising biomarker for cervical cancer but also provides insight into the possible role of DNMT3L in cancer development.