Recombinant Simian Virus 40 Major Capsid VP1 protein is a Simian Virus 40 Full Length protein, expressed in Saccharomyces cerevisiae, with >85% purity and suitable for ELISA, WB, SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application ELISA | Reactivity Reacts | Dilution info 0.50000-5.00000 µg/mL | Notes - |
Application WB | Reactivity Reacts | Dilution info 1.00000-5.00000 µg/mL | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info 4.2 µg/mL | Notes - |
Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Binds to N-glycolylneuraminic analog of the ganglioside GM1 on the cell surface to provide virion attachment to target cell (PubMed:18353982). Once attached, the virion is internalized by caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating (PubMed:17981119). Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus (PubMed:17981119). Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. The assembly takes place in the cell nucleus. Encapsulates the genomic DNA and participates in rearranging nucleosomes around the viral DNA. The viral progenies exit the cells by lytic release.
Simian Virus 40 Major Capsid VP1
Major capsid protein VP1, Major structural protein VP1
Recombinant Simian Virus 40 Major Capsid VP1 protein is a Simian Virus 40 Full Length protein, expressed in Saccharomyces cerevisiae, with >85% purity and suitable for ELISA, WB, SDS-PAGE.
Constituents: PBS
Purified by ultracentifugation
Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Binds to N-glycolylneuraminic analog of the ganglioside GM1 on the cell surface to provide virion attachment to target cell (PubMed:18353982). Once attached, the virion is internalized by caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating (PubMed:17981119). Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus (PubMed:17981119). Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. The assembly takes place in the cell nucleus. Encapsulates the genomic DNA and participates in rearranging nucleosomes around the viral DNA. The viral progenies exit the cells by lytic release.
Belongs to the polyomaviruses coat protein VP1 family.
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SDS-PAGE showing ab74565 at approximately 44kDa (4.2μg/lane)
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