产品名称：Anti-HIV1 gp120/FITC抗体

Anti-HIV1 gp120/FITC抗体

产品编号YB0241R-FITC

英文名称Anti-HIV1 gp120/FITC

中文名称FITC标记的艾滋病病毒抗体

别    名HIV-1 ENV (gp120); HIV1 gp120; HIV1gp120; HIV-1 gp120; Envelope surface glycoprotein gp120; Glycoprotein 120; gp120; gp120 glycoprotein; Human Immunodeficiency Virus 1; SU; Surface protein; ENV_HV1MN; Envelope glycoprotein gp160; Env polyprotein; Surface protein gp120; SU.  

Anti-HIV1 gp120/FITC抗体

说 明 书100ul  

研究领域**及病毒  

抗体来源Rabbit

克隆类型Polyclonal

交叉反应 HIV-1 M:B_MN

产品应用IF=1:50-200  

not yet tested in other applications.

optimal dilutions/concentrations should be determined by the end user.

分 子 量53/91kDa

Anti-HIV1 gp120/FITC抗体性    状Lyophilized or Liquid

浓    度1mg/ml

免 疫 原KLH conjugated synthetic peptide derived from HIV1 Surface protein gp120

亚    型IgG

纯化方法affinity purified by Protein A

储 存 液0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.

保存条件Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.

Anti-HIV1 gp120/FITC抗体

产品介绍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).

Function:

The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide.

Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediatesAnti-HIV1 gp120/FITC抗体 T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS.

The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells.

The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).

The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface.

The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus-infected cells, on the point of undergoing apoptosis, fuse with CD4-expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion.

The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves.

Subunit:

The mature envelope protein (Env) consists of a homotrimer of non-covalently associated gp120-gp41 heterodimers. The resulting complex protrudes from the virus surface as a spike. There seems to be as few as 10 spikes on the average virion. Surface protein gp120 interacts with human CD4, CCR5 and CXCR4, to form a P4HB/PDI-CD4-CXCR4-gp120 complex. Gp120 also interacts with the C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts with human ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in rapid activation of integrin ITGAL/LFA-1, which facilitate efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-associated heparan sulfate; this interaction increases virus infectivity on permissive cells and may be involved in infection of CD4- cells.

Subcellular Location:

Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein (Potential). Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.

Surface protein gp120: Virion membrane; Peripheral membrane protein (By similarity). Host cell membrane; Peripheral membrane protein (By similarity). Host endosome membrane; Peripheral membrane protein (Potential). Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.

Post-translational modifications:

Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor.

Database links:

UniProtKB/Swiss-Prot: P05877

Important Note:

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

人类**缺陷病毒Ⅰ型(HIV-1)的包膜糖蛋白gp120、gp41

HIV感染后可刺激机体产生囊膜蛋白（Gp120,Gp41）抗体

病毒呈球形，直径100～120nm，电镜下可见一致密的圆锥状核心，内含病毒RNA分子和酶（逆转录酶、整合酶、蛋白酶），病毒外层囊膜系双层脂质蛋白膜，其中嵌有gp120和gp41，分别组成刺突和跨膜蛋白。