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Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Additionally we are shipping Protein Arginine Methyltransferase 8 Antibodies (57) and and many more products for this protein.
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PRMT8 in human embryonic stem cells plays an important role not only in maintaining pluripotency but also in controlling mesodermal differentiation.
Mutational defects in PRMT8 is not the cause of frontotemporal lobar degeneration.
automethylation of the N terminus likely regulates PRMT8 activity by decreasing the affinity of the enzyme for AdoMet (show MAT1A Proteins)
wild type FUS (FUS (show FUS Proteins)-WT) specifically interacts with protein arginine methyltransferases 1 and 8 (PRMT1 (show PRMT1 Proteins) and PRMT8) and undergoes asymmetric dimethylation
PRMT8 is an active arginine methyltransferase that is membrane-associated and tissue-specific
PRMT8 N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers.
The interaction between PRMT8 and the EWS (show EWSR1 Proteins) protein was charcterized.
EWS (show EWSR1 Proteins) is a substrate for PRMT8, as efficient as for PRMT1 (show PRMT1 Proteins)
prmt8 may play important roles non-overlapping with prmt1 (show PRMT1 Proteins) in embryonic and neural development depending on its specific N-terminus.
Together, our findings establish important roles for PRMT8 in regulating neuron function and cognition in the mammalian brain.
human dermal fibroblast cells express a novel PRMT8 mRNA variant.
Prmt8 is involved in synaptic maturation and is a modulator of developmental neuroplasticity.
besides its known function in nervous system, Prmt8 could play a role in pluripotent stem cells
PRMT8 is a neuron-specific nuclear enzyme broadly distributed in the CNS neurons and the N-terminus does not contain the glycine end for myristoylation target
PRMT8 is chiefly involved in the somatosensory and limbic systems, and a part of motor system of the brain.
Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Arginine methylation is involved in a number of cellular processes, including DNA repair, RNA transcription, signal transduction, protein compartmentalization, and possibly protein translation (Lee et al., 2005
protein arginine methyltransferase 8
, HMT1 hnRNP methyltransferase-like 4
, HMT1 hnRNP methyltransferase-like 3
, heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
, protein arginine N-methyltransferase 4
, protein arginine N-methyltransferase 8
, protein arginine N-methyltransferase 8-B
, heterogeneous nuclear ribonucleoprotein methyltransferase-like 4