Human Enterovirus 71 VP0 ( VP4-VP2 )Protein
A DNA sequence
Human Enterovirus 71
> 72 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the
Samples are stable for up to twelve months from date of
Predicted N terminal:
Lyophilized from sterile 50 mM Tris, 100mM NaCl, 2 mM GSH, 0.5 mM PMSF, pH 8.0
Store it under sterile conditions at -70℃ . It is recommended that
A hardcopy of COA with reconstitution instruction is
Human enterovirus 71
genome polyprotein is a member of the picornaviruses polyprotein family. It
contains two peptidase C3 domains, one RdRp catalytic domain,
one SF3 helicase domain. Genome polyprotein is cleaved into the following
12 chains: Protein VP0 (VP4-VP2), Protein VP4 (P 1A ), Protein VP2 (P1B), Protein VP3 (P 1C ), Protein VP1 (P1D), Picornain 2A (P 2A ), Protein 2B (P2B), Protein 2C (P 2C ), Protein 3A
(P 3A ), Protein 3B (P3B),
Picornain 3C (Protease 3C ) and RNA-directed RNA polymerase 3D-POL
(P3D-POL). VP0 precursor is a component of immature procapsids. Capsid proteins
VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand
RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1,
VP2 and VP3. All the three latter proteins contain a beta-sheet structure
called beta-barrel jelly roll. Together they form an icosahedral capsid
composed of 60 copies of each VP1, VP2, and VP3, with a diameter of
approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas
VP2 and VP3 are located at the quasi-sixfold axes.
Brown B.A., et al., 1995, Virus Res. 39:195-206.
Tang W.-F. et al., 2007, J. Biol. Chem. 282:5888-5898.
et al., 2008, Virus Res. 131 (2):250-9.