Anti-mono and dimethyl Arginine antibody [7E6]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Mono and dimethyl arginine also known as methylarginine are modified forms of the amino acid arginine. This modification known as arginine methylation involves the addition of one (mono) or two (di) methyl groups to the nitrogen atoms of arginine residues in proteins. This process is mediated by protein arginine methyltransferases (PRMTs) and affects the physicochemical properties of proteins altering their function. Methylarginine is found in various cellular compartments including the nucleus and cytoplasm and is common in eukaryotic cells.

Biological function summary

Arginine methylation influences protein-protein interactions RNA binding and signal transduction. Methylated arginine residues often form part of larger protein complexes that regulate transcriptional processes. As a result mono and dimethyl arginine residues play critical roles in gene expression and act as regulators in signal transduction pathways. Additionally these modifications impact the splicing of pre-mRNA by altering the interaction with splicing factors.

Pathways

Arginine methylation participates in pathways like signal transduction and gene regulation. It has strong connections with proteins like histones and transcription factors which play functional roles in gene expression control. For example PRMTs methylate histones which affects the transcriptional state of chromatin. Methylated arginine residues also interact with the PI3K/Akt pathway which is important for cell growth and survival.

Associated diseases and disorders

Irregularities in arginine methylation have links with cancer and cardiovascular diseases. Abnormal methylation patterns can disrupt normal cell regulation contributing to oncogenesis and tumor progression. Proteins such as PRMT1 and CARM1 associated with methylated arginine are often implicated in these pathological conditions. In cardiovascular contexts asymmetric dimethylarginine (ADMA) a competitive inhibitor of nitric oxide synthase can contribute to endothelial dysfunction playing a role in the development of atherosclerosis.