emopamil binding protein (EBP) (NM_006579) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC201706L2V

Lenti ORF particles, EBP (mGFP-tagged) - Human emopamil binding protein (sterol isomerase) (EBP), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: emopamil binding protein
• Synonyms: CDPX2; CHO2; CPX; CPXD; MEND
• Mammalian Cell Selection: None
• Vector: pLenti-C-mGFP
• ACCN: NM_006579
• ORF Size: 690 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC201706).
• 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_006579.1
• RefSeq Size: 1191 bp
• RefSeq ORF: 693 bp
• Locus ID: 10682
• UniProt ID: Q15125
• Cytogenetics: Xp11.23
• Protein Families: Druggable Genome, Transmembrane
• Protein Pathways: Metabolic pathways, Steroid biosynthesis
• MW: 26.4 kDa
• Gene Summary: The protein encoded by this gene is an integral membrane protein of the endoplasmic reticulum. It is a high affinity binding protein for the antiischemic phenylalkylamine Ca2+ antagonist [3H]emopamil and the photoaffinity label [3H]azidopamil. It is similar to sigma receptors and may be a member of a superfamily of high affinity drug-binding proteins in the endoplasmic reticulum of different tissues. This protein shares structural features with bacterial and eukaryontic drug transporting proteins. It has four putative transmembrane segments and contains two conserved glutamate residues which may be involved in the transport of cationic amphiphilics. Another prominent feature of this protein is its high content of aromatic amino acid residues (>23%) in its transmembrane segments. These aromatic amino acid residues have been suggested to be involved in the drug transport by the P-glycoprotein. Mutations in this gene cause Chondrodysplasia punctata 2 (CDPX2; also known as Conradi-Hunermann syndrome). [provided by RefSeq, Jul 2008]