DYNLL1 (NM_001037494) Human Tagged ORF Clone Lentiviral Particle

SKU RC219822L4V

Lenti ORF particles, DYNLL1 (mGFP-tagged) - Human dynein, light chain, LC8-type 1 (DYNLL1), transcript variant 1, 200ul, >10^7 TU/mL

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Target Symbol: DYNLL1
• Synonyms: DLC1; DLC8; DNCL1; DNCLC1; hdlc1; LC8; LC8a; PIN
• 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(RC219822).
• ACCN: NM_001037494
• ORF Size: 267 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_001037494.1
• RefSeq Size: 820 bp
• RefSeq ORF: 270 bp
• Locus ID: 8655
• UniProt ID: P63167
• Cytogenetics: 12q24.31
• MW: 10.2 kDa
• Summary: Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized. [provided by RefSeq, Jul 2008]