Prmt7 (NM_145404) Mouse Tagged ORF Clone Lentiviral Particle
CAT#: MR210073L4V
- LentiORF®
Lenti ORF particles, Prmt7 (GFP-tagged) - Mouse protein arginine N-methyltransferase 7 (Prmt7), 200ul, >10^7 TU/mL
Lentiviral Particles: DDK w/ Puro
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Specifications
Product Data | |
Type | Mouse Tagged ORF Clone Lentiviral Particle |
Tag | mGFP |
Symbol | Prmt7 |
Synonyms | 4933402B05Rik; BC006705 |
Mammalian Cell Selection | Puromycin |
Vector | pLenti-C-mGFP-P2A-Puro |
ACCN | NM_145404 |
ORF Size | 2079 bp |
Sequence Data |
The ORF insert of this clone is exactly the same as(MR210073).
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OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Reference Data | |
RefSeq | NM_145404.1, NP_663379.1 |
RefSeq Size | 2269 bp |
RefSeq ORF | 2079 bp |
Locus ID | 214572 |
UniProt ID | Q922X9 |
Cytogenetics | 8 D3 |
Gene Summary | 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. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo (By similarity).[UniProtKB/Swiss-Prot Function] |
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