The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Protein concentration is above or equal to 0.05 mg/ml.
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Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 8.00 Constituents: 0.31% Glutathione, 0.79% Tris HCl
72 kDa ICln binding protein
72 kDa ICln-binding protein
Histone synthetic lethal 7, S. cerevisiae, homolog of
Histone-arginine N-methyltransferase PRMT5
HMT1 hnRNP methyltransferase like 5
HOMOLOG OF; SKB1
Jak-binding protein 1
Protein arginine methyltransferase 5
Protein arginine N methyltransferase 5
Protein arginine N methyltransferase 5 N terminally processed
Protein arginine N-methyltransferase 5
S. POMBE HOMOLOG OF; SKB1
SHK1 KINASE BINDING PROTEIN 1
Shk1 kinase binding protein 1 homolog
Shk1 kinase-binding protein 1 homolog
Shk1 kinase/binding protein 1, S. pombe, homolog of
SKB1: SKB1 homolog (S. pombe)
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10.
Belongs to the protein arginine N-methyltransferase family.
Disulfide bonds and non-covalent association mediate homooligomers formation.