DEGS1 (NM_003676) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC212803L4V

Lenti ORF particles, DEGS1 (mGFP-tagged) - Human degenerative spermatocyte homolog 1, lipid desaturase (Drosophila) (DEGS1), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: DEGS1
• Synonyms: DEGS; DEGS-1; Des-1; DES1; FADS7; HLD18; MIG15; MLD
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_003676
• ORF Size: 969 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC212803).
• 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_003676.2
• RefSeq Size: 2101 bp
• RefSeq ORF: 972 bp
• Locus ID: 8560
• UniProt ID: O15121
• Cytogenetics: 1q42.11
• Domains: FA_desaturase
• Protein Families: Druggable Genome, Transmembrane
• Protein Pathways: Metabolic pathways, Sphingolipid metabolism
• MW: 37.9 kDa
• Gene Summary: This gene encodes a member of the membrane fatty acid desaturase family which is responsible for inserting double bonds into specific positions in fatty acids. This protein contains three His-containing consensus motifs that are characteristic of a group of membrane fatty acid desaturases. It is predicted to be a multiple membrane-spanning protein localized to the endoplasmic reticulum. Overexpression of this gene inhibited biosynthesis of the EGF receptor, suggesting a possible role of a fatty acid desaturase in regulating biosynthetic processing of the EGF receptor. [provided by RefSeq, Mar 2010]