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Recombinant HIV-1 [HIV-1/Clade C (16055)] GP120  pdf  pdf  pdf


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Synonym

GP120,GP120-CN54

Source

Recombinant HIV-1 [HIV-1/Clade C (16055)] GP120, Thr 34 - Arg 506 (Accession # ABL67444.1) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

GP120 (Thr 34-Arg 506)ABL67444.1

polyhistidine

HIV-1 [HIV-1/Clade C (16055)] GP120 is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 54 kDa. The predicted N-terminus is Thr 34. The reducing (R) protein migrates as 65-110 kDa in SDS-PAGE due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Trehalose is added as protectant before lyophilization.

Contact us for customized product form or formulation.

Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C).

 

SDS-PAGE


Recombinant HIV-1 [HIV-1/Clade C (16055)] GP120
HIV-1 [HIV-1/Clade C (16055)] GP120 on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
 
 

Background

Human Immunodeficiency Virus (HIV) can be divided into two major types, HIV type 1 (HIV-1) and HIV type 2 (HIV-2). HIV-1 is related to viruses found in chimpanzees and gorillas living in western Africa. HIV-2 is related to viruses found in sooty mangabeys. HIV-1 viruses may be further divided into groups. The HIV-1 group M viruses predominate and are responsible for the AIDS pandemic. Some of the HIV-1 group M subtypes are known to be more virulent or are resistant to different medications. HIV-2 viruses are thought to be less virulent and transmissible than HIV-1 M group viruses. Envelope glycoprotein GP120 (or gp120) is the name of the glycoprotein which forms the spikes sticking out of a HIV virus particle. gp120 is essential for virus entry into cells as it plays a vital role in seeking out specific cell surface receptors for entry. Three gp120s, bound as heterodimers to a transmembrane glycoprotein, gp41, are thought to combine in a trimer to form the envelope spike, which is involved in virus-cell attachment. One half of the molecular weight of gp120 is due to the carbohydrate side chains (the "glyco-" in "glycoprotein"). These are sugar residues which form something almost like a sugar "dome" over the gp120 spikes. This dome prevents gp120 from being recognised by the human immune response. As the HIV virus and the human CD4 cell come together, the gp120 binding site "snaps open" at the last minute.The glycoprotein gp120 is anchored to the viral membrane, or envelope, via non-covalent bonds with the transmembrane glycoprotein, gp41. It is involved in entry into cells by binding to CD4 receptors, particularly helper T-cells. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

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References