ELOVL2 (NM_017770) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC209232L1V

Lenti ORF particles, ELOVL2 (Myc-DDK tagged) - Human ELOVL fatty acid elongase 2 (ELOVL2), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: Myc-DDK
• Symbol: ELOVL2
• Synonyms: SSC2
• Mammalian Cell Selection: None
• Vector: pLenti-C-Myc-DDK
• ACCN: NM_017770
• ORF Size: 888 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC209232).
• 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_017770.2, NP_060240.2
• RefSeq Size: 4079 bp
• RefSeq ORF: 891 bp
• Locus ID: 54898
• UniProt ID: Q9NXB9
• Cytogenetics: 6p24.2
• Domains: ELO
• Protein Families: Transmembrane
• Protein Pathways: Biosynthesis of unsaturated fatty acids
• MW: 34.6 kDa
• Gene Summary: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.[UniProtKB/Swiss-Prot Function]