ERVW-1 Polyclonal Antibody

Cat.#: 163235

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Product Information

  • Product Name
    ERVW-1 Polyclonal Antibody
  • Documents
  • Description
    Polyclonal antibody to ERVW-1
  • Tested applications
    WB
  • Species reactivity
    Human, Mouse
  • Alternative names
    ERVW-1 antibody; ENV antibody; ENVW antibody; ERVWE1 antibody; HERV-7q antibody; HERV-W-ENV antibody; HERV7Q antibody; HERVW antibody; HERVWENV antibody; syncytin-1 antibody
  • Isotype
    Rabbit IgG
  • Preparation
    Antigen: A synthetic peptide corresponding to a sequence within amino acids 1-100 of human ERVW-1 (NP_001124397.1).
  • Clonality
    Polyclonal
  • Formulation
    PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
  • Storage instructions
    Store at -20℃. Avoid freeze / thaw cycles.
  • Applications
    WB 1:500 - 1:2000
  • Validations

    Western blot - ERVW-1 Polyclonal Antibody

    Western blot - ERVW-1 Polyclonal Antibody

    Western blot analysis of extracts of various cell lines, using ERVW-1 antibody at 1:1000 dilution.Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Basic Kit .Exposure time: 3s.

  • Background
    This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5.; Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of membranes.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"