Anti-METTL4 / Methyltransferase-like protein 4

In 1X PBS, pH 7.4, with 0.09% sodium azide. METTL4 is a protein that belongs to the methyltransferase-like family, which is involved in the transfer of methyl groups onto other molecules, such as DNA, RNA, and proteins. The exact function of METTL4 is still not fully understood, but recent studies have suggested that it may be involved in regulating gene expression and protein synthesis. Research has shown that METTL4 is expressed in a wide range of tissues and cell types, indicating its importance in normal physiological functions. Its dysregulation has been linked to various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Protein function: N(6)-adenine-specific methyltransferase that can methylate both RNAs and DNA (PubMed:31913360, PubMed:32183942). Acts as a N(6)- adenine-specific RNA methyltransferase by catalyzing formation of N6,2'-O-dimethyladenosine (m6A(m)) on internal positions of U2 small nuclear RNA (snRNA): methylates the 6th position of adenine residues with a pre-deposited 2'-O-methylation (PubMed:31913360). Internal m6A(m) methylation of snRNAs regulates RNA splicing (PubMed:31913360). Also able to act as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)- methyladenosine) (PubMed:32183942). The existence of N(6)- methyladenosine (m6A) on DNA is however unclear in mammals, and additional evidences are required to confirm the role of the N(6)- adenine-specific DNA methyltransferase activity of METTL4 in vivo (PubMed:32203414). Acts as a regulator of mitochondrial transcript levels and mitochondrial DNA (mtDNA) copy number by mediating mtDNA N(6)-methylation: m6A on mtDNA reduces transcription by repressing TFAM DNA-binding and bending (PubMed:32183942). N(6)-methyladenosine deposition by METTL4 regulates Polycomb silencing by triggering ubiquitination and degradation of sensor proteins ASXL1 and MPND, leading to inactivation of the PR-DUB complex and subsequent preservation of Polycomb silencing. [The UniProt Consortium]