About Anti-gp120/gp160 (HIV-1/Clade A) Rabbit Polyclonal Antibody

The HIV-1 envelope glycoprotein (Env) is synthesized as the precursor gp160, which is proteolytically cleaved into the surface glycoprotein gp120 and the transmembrane glycoprotein gp41. The gp120 subunit mediates viral attachment to the CD4 receptor and the chemokine co-receptors CCR5 or CXCR4, while gp41 promotes membrane fusion and viral entry into host cells. As the only viral protein exposed on the virion surface, gp120/gp160 is the principal target of neutralizing antibodies and remains a major focus of HIV vaccine development, therapeutic antibody discovery, and studies of viral entry and immune responses. HIV-1 Clade A is prevalent in parts of East Africa, Central Asia, and Eastern Europe, making Clade A-specific reagents important for regional epidemiological studies and vaccine research.

eEnzyme's Anti-gp120/gp160 (HIV-1/Clade A) Rabbit Polyclonal Antibody is generated by in vivo genetic immunization using an in vivo expressed gp140 envelope protein (amino acids 1–486) from HIV-1 Clade A (GenBank accession AF084657) as the immunogen. This strategy produces high-affinity antibodies that recognize the native conformation of the HIV-1 envelope glycoprotein with its physiologically relevant folding and glycosylation. The antibody specifically reacts with HIV-1 Clade A gp120/gp160 proteins, is immunogen affinity-purified, and is suitable for Western blotting, ELISA, immunofluorescence (IF), immunocytochemistry (ICC), immunoprecipitation (IP), and other immunological assays. It provides a valuable reagent for HIV research, recombinant protein characterization, vaccine development, and diagnostic assay development.

Applications

Biological Significance of HIV-1 gp120/gp160

The HIV-1 Env glycoprotein is indispensable for viral infection by mediating receptor recognition and membrane fusion. During viral maturation, gp160 is cleaved into gp120 and gp41, which assemble into trimeric envelope spikes on the virion surface. Binding of gp120 to CD4 induces conformational changes that enable interaction with CCR5 or CXCR4, ultimately activating gp41 to drive membrane fusion. Because gp120/gp160 contains both conserved and highly variable antigenic regions, it is the primary target of broadly neutralizing antibodies and remains central to HIV vaccine design, therapeutic antibody development, and structural studies of the viral envelope. Clade A-specific antibodies are particularly valuable for detecting recombinant and native envelope proteins, evaluating vaccine candidates based on Clade A isolates, monitoring Env expression, and supporting HIV immunology and virology research.