Biochem/physiol Actions

Envelope glycoprotein GP120 (or gp120) is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Tun-Hou Lee and Myron Essex of the Harvard School of Public Health in 1988. The protein′s name is derived from its apparent molecular weight of 120 kDa. The gp120 protein is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and the CD4 receptor. The presence of gp120 is associated with higher levels of plasma IL-6, IL-10, and TNF-α, which may contribute to immune dysfunction during early HIV infection.

General description

Recombinant human glycoprotein 120 (gp120) is expressed in human HEK 293 cells as an C-terminally his-tagged glycoprotein with a calculated molecular mass of 55 kDa (amino acids Lys33-Arg511, with a C-terminal 8-His tag). The DTT-reduced protein migrates as a 100-130 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding.

Physical form

Lyophilized from 0.22 µm filtered solution in PBS, pH7.4.