Anti-H7N9 NA蛋白質  




40108-V07H操作手冊


H7N9
(A/Anhui/1/2013) NA / Neuraminidase Protein Product Information
























Synonym :




NA




Protein Construction:




A DNA sequence
encoding the Influenza A virus (A/Anhui/1/2013(H7N9)) (AGI60300.1)
neuraminidase (His36-Leu465) was expressed with an N-terminal polyhistidine
tag.




Source:




Influenza A virus




Expression Host:




Human Cells








H7N9
(A/Anhui/1/2013) NA / Neuraminidase Protein
QC Testing







































Purity:




> 95 % as determined by SDS-PAGE




SDS-PAGE:

 



H7N9 NA protein




Bio-activity:




Measured by its ability to cleave a fluorogenic
substrate, 2’ -(4-Methylumbelliferyl)-α-D-N-acetylneuraminic
acid.

The specific activity is >500 pmole/min/μg.




Endotoxin:




< 1.0 EU per μg of the protein as determined by the
LAL method




Stability:




Samples are stable for up to twelve months from date of
receipt at -70




Predicted N terminal:




His




Molecular Mass:




The recombinant
neuraminidase of Influenza A virus (A/Anhui/1/2013(H7N9)) comprises 448 amino
acids and has a predicted molecular mass of 50.6 kDa. The apparent molecular
mass of the protein is approximately 61-69 kDa in SDS-PAGE under reducing
conditions.




Formulation:




Lyophilized from sterile PBS, pH 7.4.




  1. Normally 5 % -
    8 % trehalose and mannitol 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.



 








H7N9
(A/Anhui/1/2013) NA / Neuraminidase Amino Acid Sequence












HHHHHHHHHH LEVLFQGPHL KPGCNCSHSQ PETTNTSQTI INNYYNETNI
TNIQMEERTS RNFNNLTKGL CTINSWHIYG KDNAVRIGES SDVLVTREPY VSCDPDECRF YALSQGTTIR
GKHSNGTIHD RSQYRALISW PLSSPPTVYN SRVECIGWSS TSCHDGKSRM SICISGPNNN ASAVVWYNRR
PVAEINTWAR NILRTQESEC VCHNGVCPVV FTDGSATGPA DTRIYYFKEG KILKWESLTG TAKHIEECSC
YGERTGITCT CRDNWQGSNR PVIQIDPVAM THTSQYICSP VLTDNPRPND PNIGKCNDPY PGNNNNGVKG
FSYLDGANTW LGRTISTASR SGYEMLKVPN ALTDDRSKPI QGQTIVLNAD WSGYSGSFMD YWAEGDCYRA
CFYVELIRGR PKEDKVWWTS NSIVSMCSST EFLGQWNWPD GAKIEYFL








H7N9 (A/Anhui/1/2013)
NA / Neuraminidase Protein Usage Guide

















Storage:




Store it under sterile conditions at -70 . It is recommended that
the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw
cycles
.




Reconstitution:




A hardcopy of COA with reconstitution instruction is
sent along with the products. Please refer to it for detailed information.








H7N9
(A/Anhui/1/2013) NA / Neuraminidase Protein Related Products & Topics







Related Areas:





Proteins:





Antibodies:







H7N9
(A/Anhui/1/2013) NA / Neuraminidase Protein Description







H7N9 is a subtype of
Influenza virus A. On April 1, 2013, the World Health Organization (WHO) first
reported 3 human infections with a new influenza A (H7N9) virus in China . Since
then, additional cases have been reported. This new H7N9 virus is an avian
(bird) influenza (flu) virus. Influenza (flu) is a respiratory infection in
mammals and birds. The virus is divided into three main types (Influenza A,
Influenza B, and Influenza C), which are distinguished by differences in two
major internal proteins (hemagglutinin (HA) and neuraminidase (NA)). The
influenza viral neuraminidase (NA) protein is a tetramer with an enzyme active
site on the head of each monomer. Subtypes are further divided into strains;
each genetically distinct virus isolate is usually considered to be a separate
strain. NA protein is a second major surface antigen of the virion.
Neuraminidase (NA) cleaves terminal sialic acid from glycoproteins or
glycolipids. Thus, it functions to free virus particles from host cell
receptors, to permit progeny virions to escape from the cell in which they
arose, and so facilitate virus spread.







References







1.                     
Suzuki T. et al., 2005, J Virol. 79: 11705-15.





2.                     
Shinya K. et al., 2006, Nature. 440 (7083): 435-6.





3.                     
Von Itzstein M. 2007, Nat Rev Drug Discov. 6: 967-74.





4.                     
Christophe F. et al., 2009, Science. 324: 1557-61.





5.                     
Marjuki H. et al., 2006, J Biol Chem. 281: 16707-15.





6.                     
Christophe F. et al., 2009, Science. 324:1557-61.





 


 

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