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Human PRMT5 / SKB1 Protein (His & FLAG Tag)

HRMT1L5,IBP72,JBP1,SKB1,SKB1Hs

Catalog Number P11074-H18H
Organism Species Human
Host Human Cells
Synonyms HRMT1L5,IBP72,JBP1,SKB1,SKB1Hs
Molecular Weight The recombinant human PRMT5 consists of 655 amino acids and predictes a molecular mass of 75 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhPRMT5 is approximately 65 kDa.
predicted N Met
SDS-PAGE
Purity > 85 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human PRMT5 (NP_006100.2) (Ala 2-Leu 637) was expressed, fused with a polyhistidine tag at the C-terminus and a Flag tag at the N-terminus.
Bio-activity
Research Area Epigenetics |Histone Modifying Enzymes |Methylation and Demethylation |Histone methylation
Formulation Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 0.5mM EDTA, 0.5PMSF, 0.5mM, TCEP, 25% glycerol
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of PRMTs. The modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. Protein arginine methyltransferase 5 (PRMT5) is a member of the protein arginine N-methyltransferases (PRMT)family, and exists as at least homodimers and homotetramers, or homooligomers mediated by disulfide bonds and non-covalent association ubiquitously. PRMT5 specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3), and thus plays a role in the assembly and biogenesis of snRNP core particles. PRMT5 methylates histone H2A and H4 'Arg-3' during germ cell development, as well as histone H3 'Arg-8', which may repress transcription. PRMT5 also methylates SUPT5H and regulates its transcriptional elongation properties. Additionally, it is also suggested that PRMT5 negatively regulates cyclin E1 promoter activity and cellular proliferation.
Reference
  • Rho. J. et al., 2001, J.Biol. Chem. 276: 11393-11401.
  • Fabbrizio, E.et al., 2002, EMBO.Rep. 3: 641-645.
  • Azzouz, T.N. et al., 2005, J.Biol. Chem. 280: 34435-34440.
  • Pal, S., et al., 2004, Mol. Cell. Biol. 24:9630-9645.
  • Herrmann, FJ. et al., 2009, Cell Sci. 122 (Pt 5): 667-77.