Anti-PRMT5 monoclonal antibody, clone QSNU6-32

Antibody Isotype

IgG2a

Clone

QSNU6-32

Species Reactivity

Human

Immunogen

Antibody was produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with PRMT5 containing the C-terminal region of the Human PRMT5 (amino acids 315-637).

Conjugate

Alternative Names

PRMT5; protein arginine N-methyltransferase 5; SKB1 homolog; Jak-binding protein 1; shk1 kinase-binding protein 1 homolog; histone-arginine N-methyltransferase PRMT5; Jbp1; Skb1;

Entrez Gene ID

UniProt ID

Antigen Description

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.

Pathway

Gene Expression, organism-specific biosystem; Metabolism of non-coding RNA, organism-specific biosystem; RNA transport, organism-specific biosystem; RNA transport, conserved biosystem; snRNP Assembly, organism-specific biosystem;