Hello, Sign in
My Account
My Account
New customer? Start here
| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| VAG0346-100 | 7 days | 100 µg | $400.00 |
Select product before adding to cart
|
||
| VAG0346-500 | 7 days | 500 µg | $1,600.00 | |||
| VAG0346-1000 | 7 days | 1000 µg | $2,240.00 |
Product Overview | |
| Name | HIV-2 gag |
|---|---|
| Description | |
| HIV-2 gag Recombinant | |
| Introduction | |
| HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids. Immunodeficiency develops more slowly with HIV-2. HIV-2 is less infectious in the early stages of the virus than with HIV-1. The infectiousness of HIV-2 increases as the virus progresses. Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion. HIV2 gp160 protein contains HIV2 Subtype A sequence, covering C4, V5, and C5 from HIV2 gp120 and extending to HIV2 gp36. | |
| Source | |
| Escherichia Coli. | |
| Physical Appearance | |
| Sterile Filtered clear solution. | |
| Formulation | |
| HIV-2 gp160 solution contains 25mM K2 ₂ CO ₃, PBS & 8M urea. | |
| Stability | |
| Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. | |
| Purity | |
| Protein is >90% pure as determined by 10% PAGE (coomassie staining). | |
| Applications | |
| Lateral flow immunoassay and ELISA test. | |
| Precautions | |
| HIV-2 gag is for research use only and not for use in diagnostic or therapeutic procedures. | |
Background |
Human Immunodeficiency Virus type 2 (HIV-2) is a closely related retrovirus to HIV-1, and it also causes AIDS. However, HIV-2 exhibits distinct clinical and virological characteristics, including a lower transmission rate and slower disease progression. Despite its relative lower prevalence compared to HIV-1, HIV-2 remains a significant public health concern, particularly in West Africa and parts of India. Understanding the molecular mechanisms underlying HIV-2 replication is crucial for developing effective antiviral strategies against this virus. The HIV-2 Gag protein plays a central role in the assembly and maturation of viral particles. Gag is a polyprotein precursor that undergoes a series of proteolytic cleavages to yield the mature structural proteins essential for viral assembly and infectivity. Research on HIV-2 Gag has been limited compared to HIV-1, and a comprehensive characterization of HIV-2 Gag recombinant is necessary to shed light on its role in viral replication. The primary objective of this study is to express and purify recombinant HIV-2 Gag protein using various expression systems. Recombinant DNA techniques will be employed to construct expression vectors harboring the HIV-2 gag gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant Gag protein will be purified using affinity chromatography or other suitable methods, allowing for subsequent biochemical and biophysical characterization. The second objective is to investigate the assembly and maturation processes of HIV-2 Gag protein. In vitro assays will be conducted to analyze the ability of the purified Gag protein to self-assemble into virus-like particles (VLPs). The formation and morphology of VLPs will be characterized using techniques such as electron microscopy and dynamic light scattering. Additionally, the effect of potential inhibitors or small molecules on Gag assembly and maturation will be evaluated. The third objective is to determine the three-dimensional structure of HIV-2 Gag recombinant through X-ray crystallography or cryo-electron microscopy. Structural information will provide crucial insights into the molecular interactions involved in Gag assembly and maturation, offering a basis for rational drug design targeting HIV-2 Gag. By characterizing the HIV-2 Gag recombinant, this research aims to enhance our understanding of the assembly and maturation processes underlying HIV-2 replication. The findings from this study may contribute to the development of novel antiretroviral strategies specifically targeting HIV-2, thereby improving the treatment options available for individuals infected with this virus. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from ADMEbio to advance their research.
Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
Thank you,
ADMEbio Team
ADMEbio welcomes feedback from our customers.
Thank you,
ADMEbio Team
