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Your Position: Home > Protein > GP41 > GP1-H51H3

HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag

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  • Synonym
    HIV-1 (HXB2) GP41,GP41
  • Source
    HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag(GP1-H51H3) is expressed from E. coli cells. It contains AA Ala 533 - Leu 856 (Accession # P04578).
    Predicted N-terminus: Met
  • Molecular Characterization
    GP41 Structure

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 44.3 kDa. The protein migrates as Band dispersion when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >85% as determined by SDS-PAGE.

  • Formulation

    Supplied as 0.2 μm filtered solution in 50 mM HEPES, 150 mM NaCl, pH7.5 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
SDS-PAGE
GP41 SDS-PAGE

HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 85% (With Star Ribbon Pre-stained Protein Marker).

Bioactivity-ELISA
 GP41 ELISA

Immobilized HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag (Cat. No. GP1-H51H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-HIV-1 GP41 Antibody, Human IgG1 (2F5) with a linear range of 0.2-16 ng/mL (QC tested).

Bioactivity-SPR
 GP41 SPR

Monoclonal Anti-HIV-1 GP41 Antibody, Human IgG1 (2F5) captured on Protein A Chip can bind HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag (Cat. No. GP1-H51H3) with an affinity constant of 0.468 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

  • Background
    Infection by HIV-1 involves the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell. The HIV-1 envelope glycoprotein that mediates fusion consists of the surface subunit gp120 and the transmembrane subunit gp41. gp120 directs virion attachment to the cell-surface receptors, and gp41 then promotes viral-cell membrane fusion. A soluble, alpha-helical, trimeric complex within gp41 composed of N-terminal and C-terminal extraviral segments has been proposed to represent the core of the fusion-active conformation of the HIV-1 envelope. Three N-terminal helices within the bundle form a central, parallel, trimeric coiled coil, whereas three C-terminal helices pack in the reverse direction into three hydrophobic grooves on the surface of the N-terminal trimer. This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry.
  • Clinical and Translational Updates

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