catalog number :
MBS596042
products type :
Recombinant Protein
products full name :
Group 2 Norovirus capsid antigen
products short name :
[Group 2 Norovirus]
products name syn :
[Recombinant Norovirus group 2 capsid protein (It forms virus like particle under non -reduced condition).]
purity :
>85% (12% SDS-PAGE, Coomassie stain. Propietary chromatographic technique).
concentration :
1.4 mg/mL
storage stability :
Upon receipt, store at -20°C . Avoid multiple freeze/ thaw cycles.
tested application :
Immunoassay (IA), Vaccine Study
image1 heading :
Testing Data (TD)
other info1 :
Protein Buffer: PBS with 1mM urea and 50mM arginine. Source: E,Coli
other info2 :
Note: Centrifuge before opening to ensure complete recovery of vial contents.
products description :
Human Norovirus has two groups, group 1 and group 2. This group 2 recombinant capsid was derived from the full length capsid 53 to 548 amino acids ( Strain:HulBeijing/06/2005/CHN, Swiss-Prot B5AHE9). The full length capsid contains two regions, S and P domains. N-terminal225 amino acids is an essential element forming icosahedron. Full length GIl capsid protein was expressed and purified from E. coli with a 6 x his tag at its C- terminus, this recombinant protein forms virus like particle (VLP), showing multiple bands on SDS-PAGE in non-reduced condition, after reduc~on, the recombinant capsid protein changes to monomer status. Expect the full length capsid protein, C-terminal PI-P2-P protein from GIl VA387 strain will become available soon. C terminal capsid plays more important role in viral function, such as viral attachement to intestinal epithelial cell and immunal reaction with the specific antibody. Receptor binding region to human histo-blood group antigens (HBGAs) and important immunal epitopes directly reacting to the specific antibody are located within capsid C-terminal. P domain expressed in bacteria can spontaneously form P dime and P particle aggregated by 12 P dimmers. P particle displays an enhanced binding ability to HBGAs compared to virus-like particle (VLP) formed by the full length capsid as well as better immunal reaction.