SMCR7L (MIEF1) (NM_019008) Human Tagged ORF Clone Lentiviral Particle

SKU RC203568L4V

Lenti ORF particles, MIEF1 (mGFP-tagged) - Human Smith-Magenis syndrome chromosome region, candidate 7-like (SMCR7L), 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Target Symbol: SMCR7L
• Synonyms: AltMIEF1; dJ1104E15.3; HSU79252; MID51; MIEF1-MP; SMCR7L
• Vector: pLenti-C-mGFP-P2A-Puro
• Mammalian Cell Selection: Puromycin
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC203568).
• ACCN: NM_019008
• ORF Size: 1389 bp
• 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.
• Shipping: Dry Ice

Reference Data

• RefSeq: NM_019008.4
• RefSeq Size: 5730 bp
• RefSeq ORF: 1392 bp
• Locus ID: 54471
• UniProt ID: Q9NQG6
• Cytogenetics: 22q13.1
• Protein Families: Transmembrane
• MW: 51.3 kDa
• Summary: Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization. Binds ADP and can also bind GDP, although with lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity and the assembly of DNM1L into long, oligomeric tubules with a spiral pattern, as opposed to the ring-like DNM1L oligomers observed in the absence of bound ADP. Does not require ADP for its function in recruiting DNM1L.[UniProtKB/Swiss-Prot Function]