Anti-Simian Rotavirus VP8抗体
产品名称： Anti-Simian Rotavirus VP8抗体
英文名称： Simian Rotavirus VP8
产品编号： YB--14618R
产品价格： null
产品产地： 中国/美国
品牌商标： Ybscience
更新时间： 2023-08-17T10:29:50
使用范围： 科研使用
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Anti-Simian Rotavirus VP8抗体
| 产品编号 | YB-14618R |
| 英文名称 | Simian Rotavirus VP8 |
| 中文名称 | 辛诺柏病毒糖VP8抗体 |
| 别 名 | Simian Rotavirus VP8/VP4; Simian Rotavirus VP8 + VP4; Outer capsid protein VP8; Hemagglutinin; VP4_ROTSS; Outer Capsid protein VP4 (Hemagglutinin); Outer capsid protein VP4; RVA s4gp1; RVAs4gp1; VP4; Outer capsid protein VP4; Outer capsid protein VP8*; Simian Rotavirus VP8*. 外层衣壳蛋白VP8; 猴轮状病毒VP8 |
| 规格价格 | 100ul/1580元 购买 200ul/2480元 购买 大包装/询价 |
| 说 明 书 | 100ul 200ul |
| 研究领域 | 细胞生物 细菌及病毒 |
| 抗体来源 | Rabbit |
| 克隆类型 | Polyclonal |
| 交叉反应 | Simian Rotavirus |
| 产品应用 | WB=1:500-2000 ELISA=1:500-1000 IHC-P=1:400-800 IHC-F=1:400-800 ICC=1:100-500 IF=1:100-500 （石蜡切片需做抗原修复） not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. |
| 分 子 量 | 26/87kDa |
| 性 状 | Lyophilized or Liquid |
| 浓 度 | 1mg/ml |
| 免 疫 原 | KLH conjugated synthetic peptide derived from Simian Rotavirus VP8:1-100/776aa |
| 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. |
| PubMed | PubMed |
| 产品介绍 | background: Simian Rotavirus VP4 (Outer Capsid protein VP4) (Hemagglutinin) functions as a spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1. VP4 is a homotrimer and adopts a dimeric appearance above the capsid surface, while forming a trimeric base anchored inside the capsid layer. The priming trypsin cleavage triggers its rearrangement into rigid spikes with approximate two-fold symmetry of their protruding parts. After an unknown second triggering event, cleaved VP4 may undergo another rearrangement, in which two VP5* subunits fold back on themselves and join a third subunit to form a tightly associated trimer, shaped like a folded umbrella. VP4 interacts with host ITGA2 (via ITAG2 I-domain); this interaction occurs when ITGA2 is part of the integrin heterodimer ITGA2/ITGB1. VP4 interacts with host integrin heterodimer TGA4/ITGB1 and ITGA4/ITGB7. Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion. Function: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). Outer capsid protein VP5*: forms the spike 'foot' and 'body'. Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment (By similarity). VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. Subunit: VP4 is a homotrimer (Potential). VP4 adopts a dimeric appearance above the capsid surface, while forming a trimeric base anchored inside the capsid layer. Only hints of the third molecule are observed above the capsid surface. It probably performs a series of molecular rearrangements during viral entry. Prior to trypsin cleavage, it is flexible. The priming trypsin cleavage triggers its rearrangement into rigid spikes with approximate two-fold symmetry of their protruding parts. After an unknown second triggering event, cleaved VP4 may undergo another rearrangement, in which two VP5* subunits fold back on themselves and join a third subunit to form a tightly associated trimer, shaped like a folded umbrella. VP5* is a homotrimer (Potential). The trimer is coiled-coil stabilized by its C-terminus, however, its N-terminus, known as antigen domain or 'body', seems to be flexible allowing it to self-associate either as a dimer or a trimer. The two- to three-fold reorganization and fold-back of VP5* may be linked to membrane penetration, by exposing its hydrophobic region. Interacts with host ITGA2 (via ITAG2 I-domain); this interaction occurs when ITGA2 is part of the integrin heterodimer ITGA2/ITGB1. Interacts with host integrin heterodimer ITGA4/ITGB1 and ITGA4/ITGB7. Subcellular Location: Outer capsid protein VP4: Virion. Host rough endoplasmic reticulum (Potential). Note=Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. Outer capsid protein VP8*: Virion. Note=Outer capsid protein. Outer capsid protein VP5*: Virion. Note=Outer capsid protein. Post-translational modifications: Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion. Similarity: Belongs to the rotavirus VP4 family. Gene ID: 7011406 Database links: Entrez Gene: 7011406 ROTSS SwissProt: P12473 ROTSS
Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications |