[Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both ''Lys-48'' and ''Lys-63''-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host RIGI, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this modifier that can no longer be attached to target proteins. Also cleaves host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly. .; [Capsid protein VP4]: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks. .; [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome . Upon acidifcation in the endosome, dissociates into pentamers . .; [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome . Mediates cell entry by attachment to an integrin receptor, usually host ITGAV/ITGB6. In addition, targets host MAVS to suppress type I IFN pathway (By similarity). Upon acidifcation in the endosome, dissociates into pentamers . .; [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome . .; [Protein 2A]: Mediates self-processing of the polyprotein by a translational effect termed ''ribosome skipping''. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally ''trimmed'' from the C-terminus of the upstream protein 1D by 3C proteinase. .; [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host endoplasmic reticulum and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. .; [Protein 2C]: Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. .; [Protein 3A]: Plays important roles in virus replication, virulence and host range. Cooperates with host DDX56 to inhibit IRF3 nuclear translocation and subsequent type I interferon production. .; [Protein 3B-1]: Covalently linked to the 5''-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer. .; [Protein 3B-2]: Covalently linked to the 5''-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer. .; [Protein 3B-3]: Covalently linked to the 5''-end0 of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer. .; [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. .; RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. .

p03306

Genome polyprotein [Cleaved into: Leader protease (Lpro) (EC 3.4.22.46); Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)],Genome polyprotein, Leader protease, Lpro, 3.4.22.46, Capsid protein VP0, VP4-VP2, Capsid protein VP4, P1A, Virion protein 4, Capsid protein VP2, P1B, Virion protein 2, Capsid protein VP3, P1C, Virion protein 3, Capsid protein VP1, P1D, Virion protein 1, Protein 2A, P2A, P52, Protein 2B, P2B, Protein 2C, P2C, 3.6.1.15, Protein 3A, P3A, Protein 3B-1, P3B-1, Genome-linked protein VPg1, Protein 3B-2, P3B-2, Genome-linked protein VPg2, Protein 3B-3, P3B-3, Genome-linked protein VPg3, Protease 3C, 3.4.22.28, Picornain 3C, P3C, Protease P20B, RNA-directed RNA polymerase 3D-POL, P3D-POL, 2.7.7.48, P56A

Foot-and-mouth disease virus (FMDV)

WB,ELISA

WB 1:500-1:2000
ELISA 1:5000-1:20000

260kD

Human

Monoclonal

FM273

IgG2a, kappa

Protein A/G purified from cell culture supernatant.

>95% as determined by SDS-PAGE.

0.01M PBS, pH 7.4.

0.85 mg/ml

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.