Recombinant Rubella Virus capsid protein is a Rubella virus strain Therien Full Length protein, expressed in Saccharomyces cerevisiae, with >90% purity and suitable for SDS-PAGE, ELISA, WB.
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info 2 µg/mL | Notes - |
Application ELISA | Reactivity Reacts | Dilution info 2 µg/mL | Notes - |
Application WB | Reactivity Reacts | Dilution info 1.00000-2.00000 µg/mL | Notes - |
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Capsid protein. Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. Spike glycoprotein E2. Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement. Spike glycoprotein E1. Class II viral fusion protein (By similarity). Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:15557740). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity).
Rubella Virus capsid
Structural polyprotein, p110
Recombinant Rubella Virus capsid protein is a Rubella virus strain Therien Full Length protein, expressed in Saccharomyces cerevisiae, with >90% purity and suitable for SDS-PAGE, ELISA, WB.
Constituents: PBS
Purified by ultracentifugation.
Capsid protein
Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidase. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism.
The Rubella Virus capsid is an important structural component of the Rubella virus particle. Sometimes called the capsid protein or capsid proteins it is involved in the assembling and packaging of the viral genome into new virions. The Rubella Virus capsid protein is around 33 kilodaltons in mass. It is expressed within infected host cells where it facilitates the initial steps of viral replication and particle formation. This capsid protein is essential for the structural integrity of the virus ensuring proper encapsulation of the viral RNA.
The Rubella Virus capsid interacts with various host cell factors to mediate processes like viral assembly and budding. It is part of a capsid protein complex which plays a role in the lifecycle of the virus by protecting the viral nucleic material. This nucleoprotein protein interacts with the host cell’s machinery influencing cell entry and immune evasion. The capsid elicits immune responses in the host which are detectable through assays such as the capsid ELISA often used in anti-rubella serological testing.
The Rubella Virus capsid is closely associated with the viral replication pathway and immune signaling pathways. It partners with other viral proteins to regulate replication ensuring successful synthesis of new virus particles. The host immune response against the capsid is significant involving pathways that trigger antibody production. The interaction of capsid proteins with host elements can modify immune responses assisting the virus in evading detection. Notable related proteins include the envelope proteins which work in tandem during the viral lifecycle.
The Rubella Virus capsid is fundamentally linked to rubella particularly congenital rubella syndrome. This capsid protein triggers immune responses that may not fully prevent infection but are important in diagnostic evaluations through tools like anti-rubella ELISA. Rubella infection can impact fetal development during pregnancy leading to severe outcomes. The interaction of the capsid with other viral components like the nucleoprotein protein is significant in the spread and pathology of the virus influencing the course of infectivity and disease manifestation.
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SDS-PAGE showing ab74574 at approximately 35kDa (2μg/lane)
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