Coxsackievirus A16 VP1 Protein (295a.a, sf9, Fc)

Coxsackievirus A16 (CVA16) can cause hand-foot-and-mouth disease (HFMD). CVA16 is a small, non-enveloped, icosahedral particle containing a single-stranded, positive-sense viral RNA genome of approximately 7.4 kb in length. CVA16 can be cleaved by viral proteases into 4 structural (VP1 to VP4) and 7 nonstructural (2A to 2C, and 3A to 3D) proteins. CVA16 interacts with its host receptors (cell surface heparan sulfate glycosaminoglycans and SCARB2 as its uncoating receptor) to enter into susceptible cells. Upon binding, CVA16 mature virions may transform to an uncoating intermediate state. Coxsackievirus A16 VP1 Protein is one of the capsid subunit protein of cleaved CVA16^[1][2]. Coxsackievirus A16 VP1 Protein (295a.a, sf9, Fc) is the recombinant Virus-derived Coxsackievirus A16 VP1 protein, expressed by Sf9 insect cells , with C-hFc labeled tag.

Coxsackievirus A16 (CVA16) can cause hand-foot-and-mouth disease (HFMD), a common acute infectious disease. CVA16 is a small, non-enveloped, icosahedral particle containing a single-stranded, positive-sense viral RNA genome of approximately 7.4 kb in length. CVA16 can be cleaved by viral proteases into 4 structural (VP1 to VP4) and 7 nonstructural (2A to 2C, and 3A to 3D) proteins^[1]. Therefore, Coxsackievirus A16 VP1 Protein is one of the capsid subunit protein of cleaved CVA16.
CVA16 interacts with its host receptors (cell surface heparan sulfate glycosaminoglycans and SCARB2, also known as LIMP-2 as its uncoating receptor) to enter into susceptible cells. Upon binding, CVA16 mature virions may transform to an uncoating intermediate state, termed the “135S-like particle” or “A-particle”, with the feature of expanded capsid, loss of pocket factor, and an enlarged two-fold opening^[2].

Virus

Sf9 insect cells

C-hFc

AAA50478.1 (G568-K862)

1461111  [NCBI]

Full Length of Pico_P1A

≥ 85%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.