About HIV-1 JR-FL gp120 Recombinant Protein

Human Immunodeficiency Virus Type 1 (HIV-1) is an enveloped retrovirus belonging to the genus Lentivirus in the family Retroviridae. The gp120 envelope glycoprotein is the surface subunit of the HIV-1 Env complex and mediates viral attachment to the CD4 receptor and chemokine co-receptors CCR5 or CXCR4, initiating viral entry into susceptible host cells. As the major surface antigen of HIV-1, gp120 is the primary target of neutralizing antibodies and has been extensively studied for HIV vaccine development and antiviral research. The JR-FL isolate is a well-characterized primary CCR5-tropic (R5) subtype B strain that closely resembles circulating clinical HIV-1 isolates and is widely used in studies of viral entry, broadly neutralizing antibodies (bNAbs), and HIV vaccine design.

eEnzyme's HIV-1 JR-FL gp120 Recombinant Protein is produced for research use and is suitable for antibody screening, receptor-binding studies, ELISA development, Western blotting, epitope mapping, structural characterization, and HIV vaccine research. This recombinant protein provides a valuable reagent for investigating HIV-1 entry mechanisms, host-virus interactions, and immune responses.

Applications

Biological Significance of HIV-1 JR-FL gp120

The JR-FL gp120 protein has become one of the most widely used HIV-1 envelope antigens because it represents a neutralization-resistant primary isolate with native antigenic properties. It has been extensively employed in structural studies of Env-receptor interactions, broadly neutralizing antibody characterization, and vaccine immunogen development. The HIV-1 JR-FL gp120 Recombinant Protein provides a valuable research tool for studying HIV biology, viral entry, antibody responses, and the development of next-generation HIV vaccines and therapeutics.