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Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Additionally we are shipping PRMT7 Proteins (8) and many more products for this protein.
Showing 10 out of 64 products:
Human Polyclonal PRMT7 Primary Antibody for EIA, IHC (p) - ABIN356532
Lee, Cook, Yang, Mirochnitchenko, Gunderson, Felix, Herth, Hoffmann, Pestka: PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. in The Journal of biological chemistry 2005
Show all 7 references for ABIN356532
Chicken Polyclonal PRMT7 Primary Antibody for WB - ABIN2778659
Gonsalvez, Tian, Ospina, Boisvert, Lamond, Matera: Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. in The Journal of cell biology 2007
Upregulation of PRMT7 in breast cancer may have a significant role in promoting cell invasion through the regulation of MMP9 (show MMP9 Antibodies).
results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers
Data indicate that two acidic residues within the double E loop, Asp (show ASIP Antibodies)-147 and Glu (show DCTN1 Antibodies)-149, confer specificity to protein arginine methyltransferase 7 (PRMT7.
reducing expression of individual PRMT7 target DNA repair genes showed that only the catalytic subunit of DNA polymerase (show POLB Antibodies), POLD1 (show POLD1 Antibodies), was able to resensitize PRMT7 knock-down cells to DNA-damaging agents.
Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues.
Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 (show PRMT5 Antibodies) and PRMT7 and present in euchromatic regions.
PRMT7 (like PRMT5 (show PRMT5 Antibodies)) is a Type II methyltransferase capable of producing symmetric dimethylarginine modifications in proteins.
that in human cells, PRMT5 (show PRMT5 Antibodies) and PRMT7 are required for Sm protein sDMA modification, and that Sm protein symmetric dimethylarginine modification is required for snRNP (show LSM2 Antibodies) biogenesis in human cells.
PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module
PRMT7 could recruit H4R3me1 and symmetric H4R3me2 to the Bcl6 (show BCL6 Antibodies) promoter. These results provide evidence for the important roles played by PRMT7 in germinal center formation.
Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions.
CTCFL (show CTCFL Antibodies) and PRMT7 may play a role in male germline imprinted gene methylation.
Prmt7 regulates epiboly by facilitating 2-OST and modulating actin cytoskeleton
Data indicate that only the N-terminal catalytic site of protein arginine methyltransferase 7 (PRMT7) is responsible for cofactor binding.
Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004
protein arginine methyltransferase 7
, [Myelin basic protein]-arginine N-methyltransferase PRMT7
, histone-arginine N-methyltransferase PRMT7
, myelin basic protein-arginine N-methyltransferase
, protein arginine N-methyltransferase 7
, arginine N-methyltransferase
, Histone-arginine N-methyltransferase PRMT7