Name :
Recombinant Human PRMT5 Protein (His & FLAG Tag)
Biological Activity :
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.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
Baculovirus-Insect Cells
Tag :
Protein Accession No. :
NCBI Gene ID :
Synonyms :
Synonyms :
protein arginine methyltransferase 5
Amino Acid Sequence :
Molecular Weight :
The recombinant Human PRMT5 consisting of 655 amino acids and has a calculated molecular mass of 75.06 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 64.8 kDa protein in SDS-PAGE under reducing conditions.
Purity :
≥ 90 % as determined by SDS-PAGE.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method
Protein Construction :
A DNA sequence encoding the Human PRMT5 (NP_006100.2) (Ala2-Leu637) was expressed with a N-terminal polyhistide-tagged FLAG tag at the N-terminus (his-FLAG).
Buffer Solution :
Supplied as sterile 20mM Tris, 300mM NaCl, 25% Glycerol,1mM TCEP, pH 8.0.Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
HRMT1L5 Protein, Human; IBP72 Protein, Human; JBP1 Protein, Human; SKB1 Protein, Human; SKB1Hs Protein, Human PRMT5 背景信息 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.
References & Citations :
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.
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