Porcine circovirus 2 Capsid protein (sf9, His)

The porcine circovirus 2 capsid protein autonomously constructs the icosahedral capsid of the viral particle, which is essential for initial attachment to host cell surface proteoglycans. Small size contributes to environmental stability and disinfectant resistance. Porcine circovirus 2 Capsid protein (sf9, His) is the recombinant Virus-derived Porcine circovirus 2 Capsid protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of Porcine circovirus 2 Capsid protein (sf9, His) is 192 a.a., with molecular weight of ~23.8 kDa.

The Porcine Circovirus 2 Capsid Protein autonomously assembles to construct the virion's icosahedral capsid with a T=1 symmetry, characterized by a very small size (17 - 22 nm in diameter) that contributes to the virus's environmental stability and resistance to certain disinfectants, including detergents. Crucial for the initial attachment to host cell surface proteoglycans, particularly heparan sulfate moieties and chondroitin sulfate B, the capsid protein facilitates the subsequent internalization of the virus through a clathrin-, caveolae-, and dynamin-independent pathway, mediated by actin and Rho-GTPase. Following attachment, the virus traffics to the nucleus, where the capsid protein binds and transports the viral genome and Rep across the nuclear envelope. It forms homomultimers and assembles in the nucleus, potentially in an immature form, before migrating to the cytoplasm upon achieving maturation as a virion. Additionally, the Capsid Protein interacts with Rep, facilitating the relocation of Rep into the nucleus.

Virus

Sf9 insect cells

C-His

O56129 (N42-P233)

/

Approximately 23.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.