癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Avian Influenza Neuraminidase Antibody
- 产品详情
- 实验流程
- 背景知识
Application 
| E |
|---|---|
| Primary Accession | Q710U6 |
| Other Accession | CAC95053, 39840718 |
| Reactivity | Virus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 51486 Da |
| Concentration (mg/ml) | 1 mg/mL |
| Conjugate | Unconjugated |
| Application Notes | Avian influenza neuriminidase antibody can be used for the detection of the avian influenza neuriminidase protein from the H5N1 strain of Avian influenza A in ELISA. It will detect 10 ng of free peptide at 1 µg/mL. |
| Other Names | Avian Influenza Neuraminidase Antibody: Neuraminidase, Neuraminidase |
|---|---|
| Target/Specificity | NA; |
| Reconstitution & Storage | Avian Influenza Neuraminidase antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
| Precautions | Avian Influenza Neuraminidase Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | NA {ECO:0000255|HAMAP-Rule:MF_04071} |
|---|---|
| Function | Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. |
| Cellular Location | Virion membrane {ECO:0000255|HAMAP- Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP- Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP- Rule:MF_04071} |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Avian Influenza Neuraminidase Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. Although it has been known that cleavage site and glycosylation patterns of the HA protein play important roles in determining the pathogenicity of H5 avian influenza viruses, it has only recently been shown that an additional glycosylation site within the globular head of the NA protein also contributes to the high virulence of the H5N1 virus.
REFERENCES
Thompson WW, Shay DK, Weintraub, et al. Mortality associated with influenza and respiratory syncytial virus in the United States. JAMA 2003; 289:179-186.
Alexander DJ. A review of avian influenza. Proceedings of the European Society for Veterinary Virology (ESVV) Symposium on Influenza Viruses of Wild and Domestic Animals. Vet. Microbiol. 2000; 74:3-13.
Shortridge KF, Zhou NN, Guan Y, et al. Characterization of avian H5N1 influenza viruses from poultry in Hong Kong. Virol. 1998; 252:331-342.
Buxton Bridges C, Katz JM, Seto WH, et al. Risk of influenza A (H5N1) infection among health care workers exposed to patients with influenza A (H5N1), Hong Kong. J. Inf. Dis. 2000; 181:344-8.
终于等到您。ABCEPTA（百远生物）抗体产品。
点击下方“我要评价 ”按钮提交您的反馈信息，您的反馈和评价是我们最宝贵的财富之一,
我们将在1-3个工作日内处理您的反馈信息。
如有疑问，联系：0512-88856768 tech-china@abcepta.com.
