Overview

  • Product name

    Recombinant Human ERVW-1 protein
  • Protein length

    Protein fragment

Description

  • Nature

    Recombinant
  • Source

    Wheat germ
  • Amino Acid Sequence
    • Species

      Human
    • Sequence

      DGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLV SLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINT
    • Amino acids

      116 to 215
    • Tags

      GST tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab162321 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot

    ELISA

  • Form

    Liquid
  • Additional notes

    Protein concentration is above or equal to 0.05 mg/ml.

    Previously labeled as HERV.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names

    • Endogenous retrovirus group W member 1
    • ENV
    • Envelope polyprotein gPr73
    • Enverin
    • ENVW
    • ERVWE1
    • HERV-7q
    • HERV-7q Envelope protein
    • HERV-W envelope protein
    • HERV-W-ENV
    • HERV-W_7q21.2 provirus ancestral Env polyprotein
    • HERV7Q
    • HERVW
    • HERVWENV
    • Syncytin
    • Syncytin 1
    • Syncytin1
    see all
  • Relevance

    Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has retained its original fusogenic properties and participates in trophoblast fusion during placenta morphogenesis. SU mediates receptor recognition. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide By similarity. Seems to recognize the type D mammalian retrovirus receptors SLC1A4 and SLC1A5, as it induces fusion of cells expressing these receptors in vitro. The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has 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
  • Cellular localization

    Transmembrane protein: Cell membrane; Single-pass type I membrane protein Surface protein: Cell membrane; Peripheral membrane protein

Images

  • ab162321 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab162321 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

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