85-6085-99　［取扱停止］Immunodeficiency Virus GP41 Protein, Recombinant, His-Tag [HIV-1/Group O] 100ug　497163

特徴

• Human immunodeficiency virus (HIV) is a retrovirus (genus Lentivirus) with a single-stranded, positive-sense RNA genome. Upon entry of the target cell, the viral RNA genome is converted to double-stranded DNA by a virally encoded reverse transcriptase that is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integrase allowing the genome to be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latent and the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated to infect other cells. Infection with HIV leads to a condition in which the immune system begins to fail, leading to opportunistic infections. HIV primarily infects cells in the human immune system including CD4 T cells, macrophages and dendritic cells. Infection subsequently results in low levels of CD4 T cells via direct viral killing of infected cells, increased rates of apoptosis in infected cells and killing of infected CD4 T cells by CD8 cytotoxic lymphocytes that recognize infected cells. When CD4 T cell numbers decline below a critical level, cell-mediated immunity is lost, and the body becomes progressively more susceptible to opportunistic infections.
• Gp41 also known as glycoprotein 41 is a subunit of the envelope protein complex of human immunodeficiency virus (HIV). It is a transmembrane protein that contains several sites within its ectodomain that are required for infection of host cells and as a result it has received much attention as a potential target for HIV vaccines. Essentially, gp41 mediates fusion between viral and cellular membranes (Chan et al., 1997). Gp41 is coded with gp120 as one gp160 by the env gene of HIV. Gp160 is then extensively glycosylated and proteolytically cleaved by a host cellular protease, furin. The high glycosylation of the env coded glycoproteins allows them to escape the human body’s immune system. Gp41 is less glycosylated that gp120 and more conserved (less prone to genetic variations). Once gp160 has been cleaved into its individual subunits, the subunits are then associated non-covalently on the surface of the viral envelope.
• When they are non-covalently bound to each other Gp41 and gp120 form the envelope spike complex, composed of a heterotrimer of three gp41 and three gp120. The complex is responsible for the attachment, fusion, and ultimately the infection of host cells. Gp120 sits on the surface of the viral envelope and gp41 is the transmembrane portion of the spike complex with part of the glycoprotein buried within the viral envelope. The membrane-proximal external region (MPER) is a highly conserved region of gp41 subunit near the viral envelope surface, and plays a key role in membrane fusion. It is seen as an attractive vaccine target using broadly neutralizing antibodies (bNAbs) or non-neutralizing, yet protective, antibodies (Liu et al., 2018).
• HIV integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. It is one of three enzymes of HIV, the others being the Reverse Transcriptase and the Protease. The enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The full length HIV-1 integrase (288aa) has three domains: the N-terminal domain has a His2Cys2 motif which chelates zinc, the core domain has the catalytic DDE motif which is required for its enzymatic activity, and the C-terminal domain has an SH3-like fold which binds DNA nonspecifically. Although all three domains are required for integration, it is thought that the catalytic core domain contains the active site responsible for catalysis of all the reactions of integration/disintegration. The C-terminal domain confers the capacity to bind both viral and host DNA. The structure and function of the N-terminal domain are presently unknown, but it contains a His2Cys2 zinc binding motif, suggesting a possible interaction with nucleic acid. HIV integrase is a 32kD protein produced from the C-terminal portion of the Pol gene product, and is an attractive target for anti-HIV drugs.
• Source:Recombinant protein corresponding to Immunodeficiency Virus GP41 Protein, fused to His-Tag at C-terminal, expressed in E. coli.
• Applications:Suitable for use in Western Blot, Lateral Flow and ELISA. Other applications not tested.
• Recommended Dilution:Optimal dilutions to be determined by the researcher.
• Molecular Weight:~13kD
• Storage and Stability:May be stored at 4°C. For long-term storage, aliquot and store at 4°C. Do not freeze. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.