About HIV-1 gp140 (JRFL Isolate) Recombinant Protein

The HIV-1 JRFL isolate is a well-characterized CCR5 (R5)-tropic primary Clade B strain that has become one of the most extensively studied HIV-1 isolates in viral entry, antibody discovery, and vaccine research. Unlike laboratory-adapted X4 strains, JRFL more closely resembles viruses responsible for primary HIV transmission and is widely used for evaluating broadly neutralizing antibodies (bnAbs), receptor interactions, and Env trimer structure. The HIV-1 envelope glycoprotein gp140 comprises the complete extracellular gp120 subunit and the ectodomain of gp41, preserving many of the conformational epitopes found on native viral Env spikes. As a result, recombinant JRFL gp140 serves as a valuable research reagent for studying HIV-1 entry, receptor binding, immune recognition, and vaccine antigen design.

eEnzyme's HIV-1 gp140 (JRFL Isolate) Recombinant Protein is expressed in HEK293 cells, producing a highly glycosylated protein with native-like post-translational modifications that closely resemble those found on authentic HIV-1 envelope glycoproteins. The purified recombinant protein exhibits high purity (>95% by SDS-PAGE) and is suitable for a broad range of immunological, biochemical, and structural applications. Owing to its preserved conformational integrity, this recombinant gp140 is ideal for ELISA, Western blotting, neutralizing antibody characterization, receptor-binding studies, vaccine antigen evaluation, and assay development. It provides researchers with a reliable reagent for investigating HIV-1 Env biology and evaluating candidate therapeutics and vaccines.

Applications

Biological Significance of HIV-1 gp140 (JRFL)

The HIV-1 envelope glycoprotein is the only viral protein exposed on the virion surface and is therefore the principal target of neutralizing antibodies. During infection, gp120 binds the CD4 receptor, followed by interaction with the CCR5 co-receptor, triggering conformational rearrangements that activate gp41 to mediate viral and host membrane fusion. Because the JRFL isolate is naturally CCR5-tropic, it serves as an excellent model for studying the earliest stages of HIV-1 transmission and infection. Its envelope glycoprotein has been widely used in the development of HIV vaccines, the discovery of broadly neutralizing antibodies, and high-resolution structural studies of native-like Env trimers. Recombinant JRFL gp140 retains many of the conformational and glycan-dependent epitopes recognized by potent neutralizing antibodies, making it an indispensable reagent for HIV-1 immunology, virology, structural biology, and therapeutic research.