Jmjd7 (NM_001114637) Mouse Tagged ORF Clone Lentiviral Particle

CAT#: MR216128L4V

Lenti ORF particles, Jmjd7 (GFP-tagged) - Mouse jumonji domain containing 7 (Jmjd7), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Mouse Tagged ORF Clone
• Tag: mGFP
• Symbol: Jmjd7
• Synonyms: MGC106779
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_001114637
• ORF Size: 948 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(MR216128).
• 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_001114637.1, NP_001108109.1
• RefSeq Size: 1383 bp
• RefSeq ORF: 951 bp
• Locus ID: 433466
• UniProt ID: P0C872
• Cytogenetics: 2
• Gene Summary: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase (PubMed:28847961) (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monoxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity).[UniProtKB/Swiss-Prot Function]