HIV-1 Transmembrane Glycoprotein (HIV-1 gp41) antibody
Quick Overview for HIV-1 Transmembrane Glycoprotein (HIV-1 gp41) antibody (ABIN648039)
Target
Reactivity
Host
Conjugate
Application
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Specificity
- A.a. 546-a.a.682 sequence from strain HxB2. Reactive with gp41 in Western blot immunoassay. Antiserum does not cross-react with human T or B cells. Antiserum has not been adsorbed to remove anti-beta-galactosidase activity.
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Characteristics
- Goat Anti-Human Immunodeficiency Virus 1 (HIV-1) gp41
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Purification
- Purified
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Isotype
- IgG
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Restrictions
- For Research Use only
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Format
- Liquid
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- HIV-1 Transmembrane Glycoprotein (HIV-1 gp41)
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Target Type
- Viral Protein
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Background
- The attachment of enveloped viruses to cells and the fusion of viral and cellular membranes are critical early events in the HIV viral infection. This process is mediated by envelope glycoproteins (gp) on the surface of the virus. The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein, gp160, is proteolytically cleaved into gp120 and gp41, which remain noncovalently associated with one another. gp120 is one of the proteins that forms the envelope of HIV. gp120 projects from the surface of HIV and binds to the CD4 molecule on helper T cells. gp120 has been a logical experimental HIV vaccine because the outer envelope is the first part of the virus that encounters antibody. gp41 is embedded in the outer envelope of HIV that anchors gp120. gp41 also plays a key role in HIV's infection of CD4+ T cells by facilitating the fusion of the viral and cell membranes. The nomenclature of the gp proteins describes their respective molecular masses (e.g., gp160, gp120, gp41). RAC2 is a plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, RAC2 binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. There are two isoforms of RAC2, isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.
Target
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