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Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. 再加上，我们可以发Protein Arginine Methyltransferase 8 蛋白 (5) 和 和数多这个蛋白质的别的产品。
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Human Polyclonal PRMT8 Primary Antibody for ELISA, WB - ABIN543362
Lee, Sayegh, Daniel, Clarke, Bedford: PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. in The Journal of biological chemistry 2005
PRMT8 in human embryonic stem cells plays an important role not only in maintaining pluripotency but also in controlling mesodermal differentiation.
Biochemical, biophysical and mutagenesis experiments demonstrated that hPRMT8 forms an octamer in solution.
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
wild type FUS (FUS-WT) specifically interacts with protein arginine methyltransferases 1 and 8 (PRMT1 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 protein was charcterized.
EWS is a substrate for PRMT8, as efficient as for PRMT1
prmt8 may play important roles non-overlapping with prmt1 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