Influenza A H5N1 (Egypt/2321-NAMRU3/2007) Neuraminidase / NA (Codon Optimized) Gene ORF cDNA clone expression plasmid, C-Myc tag

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Influenza A H5N1 (Egypt/2321-NAMRU3/2007) Neuraminidase / NA (Codon Optimized) Gene ORF cDNA clone expression plasmid, C-Myc tag: 产品信息

基因
种属
H5N1
基因长度
1350 bp
序列特征
A number of silent mutations were introduced into the DNA sequence in order to increase its protein expression level in mammalian cell system. The translated amino acid sequence is identical with ACJ53852.1.
产品特征
Full length Clone DNA of Influenza A H5N1 (Egypt/2321-NAMRU3/2007) Neuraminidase with C terminal Myc tag.
质粒
启动子
Enhanced CMV promoter
载体
标签序列
Myc Tag Sequence: GAGCAGAAACTCATCTCAGAAGAGGATCTG
测序引物
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
质控
The plasmid is confirmed by full-length sequencing.
筛选
细菌筛选抗性
Kanamycin
细胞筛选抗性
Hygromycin
应用
Stable or Transient mammalian expression
储存 & 运输
运输方式
Each tube contains lyophilized plasmid.
储存条件
The lyophilized plasmid can be stored at ambient temperature for three months.

Influenza A H5N1 (Egypt/2321-NAMRU3/2007) Neuraminidase / NA (Codon Optimized) Gene ORF cDNA clone expression plasmid, C-Myc tag: 别称

NA cDNA ORF Clone, H5N1

Neuraminidase/NA 背景信息

Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies.
参考文献
  • Sardet C., et al.,(1989), Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter. Cell 56:271-280.
  • Sardet C., et al., (1990), Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.Science 247:723-726.
  • Tse C.-M., et al.,(1991), Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger.EMBO J. 10:1957-1967.

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