Thermo Fisher Scientific AEV polyprotein Polyclonal Antibody

Applications

ELISA

• Tested Dilution: 1:5,000–1:10,000
• Publications: [References not provided]

Product Specifications

Target Information

Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive-strand RNA genome. Each protein contains a beta-sheet structure called the beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Å.
VP1 is located at the 12 fivefold axes, while VP2 and VP3 are positioned at the quasi-sixfold axes.

Protein VP0 acts as a precursor in immature procapsids. Its N-terminal domain, VP4, is essential for assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated.
Protein 2B and its precursor 2BC affect membrane integrity and increase membrane permeability.
Protein 2C associates with and induces structural rearrangements of intracellular membranes, displaying RNA-binding, nucleotide-binding, and NTPase activities.
Protein 3A serves as a membrane anchor via its hydrophobic domain.
Protein 3B is covalently linked to the 5′ end of both positive-strand and negative-strand genomic RNAs, acting as a genome-linked replication primer.
Protease 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. It also binds viral RNA, influencing genome replication. RNA and substrate bind cooperatively to the protease.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replication-specific signals.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.