Influenza A H1N1 (A/Michigan/45/2015) Neuraminidase / NA (His Tag)

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Influenza A H1N1 (A/Michigan/45/2015) Neuraminidase / NA (His Tag): 製品情報

純度
> 90 % as determined by SDS-PAGE.
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
活性
Testing in progress
タンパク質の構築
A DNA sequence encoding the Influenza A virus (A/Michigan/45/2015 (H1N1pdm09)) neuraminidase (translated amino acids of EPI859651) (His36-Lys469) was expressed with a polyhistidine tag at the N-terminus.
EP No.
発現ホスト
HEK293 Cells
H1N1
予測N末端
His
分子量
The recombinant Influenza A virus (A/Michigan/45/2015 (H1N1pdm09)) NA consists of 453 amino acids and predicts a molecular mass of 50.2 kDa.
バッファー
Lyophilized from sterile PBS, pH 7.4.
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
配送
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
安定性 & 保存条件
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
再構成
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

Influenza A H1N1 (A/Michigan/45/2015) Neuraminidase / NA (His Tag): 画像

Influenza A H1N1 (A/Michigan/45/2015) Neuraminidase / NA (His Tag): 別名

NA Protein, H1N1

Neuraminidase / NA 背景情報

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 own cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of 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 which 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. Monoclonal or polyclonal antibody can be raised with protein based antigen or peptide based antigen. Antibody raised with protein based antigen could have better specificity and/or binding affinity than antibody raised with peptide based antigen, but 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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