ERO1L (ERO1A) (NM_014584) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC203840L4V

Lenti ORF particles, ERO1L (mGFP-tagged) - Human ERO1-like (S. cerevisiae) (ERO1L), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: ERO1L
• Synonyms: ERO1-alpha; ERO1-L; ERO1-L-alpha; Ero1alpha; ERO1L; ERO1LA
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_014584
• ORF Size: 1404 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC203840).
• 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_014584.1
• RefSeq Size: 3334 bp
• RefSeq ORF: 1407 bp
• Locus ID: 30001
• UniProt ID: Q96HE7
• Cytogenetics: 14q22.1
• Domains: ERO1
• Protein Pathways: Vibrio cholerae infection
• MW: 54.4 kDa
• Gene Summary: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.[UniProtKB/Swiss-Prot Function]