Overview

  • Product name
    Recombinant Human HERV-FRD protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      MGLLLLVLILTPSLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSS TETPGTAYPASPREWTSIEAELHISYRWDPNLKGLMRPANSLLSTVKQDF PDIRQKPPIFGPIFTNINLMGIAPICVMAKRKNGTNVGTLPSTVCNVTFT VDSNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSSRFCQGRPSSC STRNFWFRPADYNQCLQISNLSSTAEWVLLDQTRNSLFWENKTKGANQSQ TPCVQVLAGMTIATSYLGISAVSEFFGTSLTPLFHFHISTCLKTQGAFYI CGQSIHQCLPSNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSPLPRVRR AIHFIPLLAGLGILAGTGTGIAGITKASLTYSQLSKEIANNIDTMAKALT TMQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQD NIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPLTGPLVSLLLLLLFG PCLLNLITQFVSSRLQAIKLQTNLSAGRHPRNIQESPF
    • Amino acids
      1 to 538
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab166518 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.
  • 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
    • EFRD1_HUMAN
    • Endogenous retrovirus group FRD member 1
    • Envelope polyprotein
    • ERVFRD-1
    • FLJ41944
    • FLJ90611
    • GLLL6191
    • HERV FRD
    • HERV FRD 6p24.1 provirus ancestral Env polyprotein
    • HERV FRD provirus ancestral Env polyprotein
    • HERV-FRD
    • HERVFRD
    • HERVFRD provirus ancestral Env polyprotein
    • MGC87585
    • SU
    • Syncytin 2
    • Syncytin B
    • Syncytin-2
    • TM
    • Transmembrane protein
    • UNQ6191
    see all
  • Function
    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. Can make pseudotypes with MLV, HIV-1 or SIV-1 virions and confer infectivity.
    SU mediates receptor recognition.
    TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane.
  • Tissue specificity
    Expressed at higher level in placenta. Expressed at lower level in adrenal, bone marrow, brain, breast, colon, kidney, lung, ovary, peripheral blood lymphocytes, prostate, skin, spleen, testis, thymus, thyroid, trachea.
  • Sequence similarities
    Belongs to the gamma type-C retroviral envelope protein family. HERV class-I FRD env subfamily.
  • Domain
    Contains the CKS-17 immunosuppressive domain present in many retroviral envelope proteins. As a synthetic peptide, it inhibits immune function in vitro and in vivo.
  • Post-translational
    modifications
    Specific enzymatic cleavages in vivo yield the mature SU and TM proteins.
    The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion.
  • Cellular localization
    Cell membrane and Virion.
  • Information by UniProt

Images

  • ab166518 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab166518 has not yet been referenced specifically in any publications.

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

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