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

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GP1-H51H3-50ug
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GP1-H51H3
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Synonyms

Envelope glycoprotein gp41/gp41 (HIV)

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: Trp

Molecular Characterization

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).

*The DDM/CHS buffer (Cat. No. DC-11) is sold separately and not included in protein, you can follow the link for product information.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>85% as determined by SDS-PAGE.

Formulation

This product is not suitable for cell based experiments due to cytotoxicity of DDM.
DDM and CHS are INDISPENSABLE to keep membrane protein soluble and active, under no circumstances should you remove DDM and CHS.
DDM/CHS buffer (DC-11) is sold separately and not included in protein, and please contact us if you need the buffer.
If glycerol is not compatible with your application, remove glycerol just before the immediate experiment, and NEVER store glycerol-free protein solution.

Supplied as 0.2 μm filtered solution in 50 mM HEPES, 150 mM NaCl, 0.05% DDM, 0.01% CHS, pH7.5 with glycerol as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.

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 th e 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.