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The protein encoded by PRMT6 belongs to the arginine N-methyltransferase family, which catalyze the sequential transfer of methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins, to form methylated arginine derivatives and S-adenosyl-L-homocysteine.
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Human PRMT6 Protein expressed in Human Cells - ABIN2004214
Hyllus, Stein, Schnabel, Schiltz, Imhof, Dou, Hsieh, Bauer: PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation. dans Genes & development 2007
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Data suggest that histone-arginine N-methyltransferase PRMT6 (PRMT6) plays an oncogenic role in prostate cancer (PCa (Montrer FLVCR1 Protéines)) and predicts for more clinically aggressive disease, constituting a potential target for patients with Prostate cancer (CRPC).
PRMT6, which was down-regulated by androgen receptors and influenced cell migration and apoptosis of germ cells, could play a potentially important role in spermatogenesis.
PRMT6 methylates tumor cell p21 (Montrer CDKN1A Protéines) at arginine 156 and promotes phosphorylation of threonine 145 on p21 (Montrer CDKN1A Protéines), increasing the cytoplasmic localization of p21 (Montrer CDKN1A Protéines) and inducing resistance to anticancer drugs.
PRMT6 influences PRC-mediated gene silencing at the rostral HOXA genes locus.
Data show that HIV-1 Tat (Montrer TAT Protéines) methylation by protein arginine methyltransferase 6 (PRMT6) can inhibit nucleolar retention.
N terminus is methylated by PRMT6 and that this critically affects the functions of pUL69 for efficient mRNA export and replication of human cytomegalovirus.
TBL1 (Montrer TBL1X Protéines) is required to protect GPS2 (Montrer GPS2 Protéines) from degradation, with methylation of GPS2 (Montrer GPS2 Protéines) by arginine methyltransferase PRMT6 regulating the interaction with TBL1 (Montrer TBL1X Protéines) and inhibiting proteasome-dependent degradation.
PRMT6 mediates cigarette smoke extract induced apoptosis and inflammation through H3R2me2a in HUVECs.
PRMT6 specifically interacts with ERalpha (Montrer ESR1 Protéines) at its ligand-binding domain.
Authors show that PRMT6 requires the activation domain, but surprisingly not the basic domain, of HIV-1 Tat (Montrer TAT Protéines) for protein interaction.
these results suggest that maternal Prmt6 is essential to early zebrafish development by directly repressing gadd45alphaa.
Six crystal structures of PRMT6 from Mus (Montrer TRPV6 Protéines) musculus, solved and refined at 1.34 A for the highest resolution structure are described.
Prmt6 is important for embryonic stem cell pluripotency and self-renewal.
The findings define a new regulator of p53 (Montrer TP53 Protéines) transcriptional regulation and define a role for PRMT6 and arginine methylation in cellular senescence.
The protein encoded by this gene belongs to the arginine N-methyltransferase family, which catalyze the sequential transfer of methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins, to form methylated arginine derivatives and S-adenosyl-L-homocysteine. This protein can catalyze both, the formation of omega-N monomethylarginine and asymmetrical dimethylarginine, with a strong preference for the latter. It specifically mediates the asymmetric dimethylation of Arg2 of histone H3, and the methylated form represents a specific tag for epigenetic transcriptional repression. This protein also forms a complex with, and methylates DNA polymerase beta, resulting in stimulation of polymerase activity by enhancing DNA binding and processivity.
arginine methyltransferase 6
, protein arginine methyltransferase 6
, HMT1 hnRNP methyltransferase-like 6
, Histone-arginine N-methyltransferase PRMT6
, protein arginine N-methyltransferase 6
, arginine N-methyltransferase, type I
, heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6
, histone-arginine N-methyltransferase PRMT6