Recombinant Polyomavirus strain RA Major Capsid VP1 protein is a Murine polyomavirus strain A2 Full Length protein, expressed in Saccharomyces cerevisiae, with >75% purity and suitable for ELISA, WB, SDS-PAGE.
>75% SDS-PAGE
Saccharomyces cerevisiae
Tag free
ELISA, WB, SDS-PAGE
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application ELISA | Reactivity Reacts | Dilution info 0.5-5 µg/mL | Notes - |
Application WB | Reactivity Reacts | Dilution info 1-5 µg/mL | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info 4.4 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. Interacts with terminal alpha(2,3)-linked sialic acids on the cell surface to provide virion attachment to target cell. 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. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Polyomavirus strain RA Major Capsid VP1
Major capsid protein VP1, Major structural protein VP1
Recombinant Polyomavirus strain RA Major Capsid VP1 protein is a Murine polyomavirus strain A2 Full Length protein, expressed in Saccharomyces cerevisiae, with >75% purity and suitable for ELISA, WB, SDS-PAGE.
>75% SDS-PAGE
Saccharomyces cerevisiae
Tag free
ELISA, WB, SDS-PAGE
No
No
Murine polyomavirus strain A2
Reconstitute in water
Constituents: PBS
Lyophilized
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. Interacts with terminal alpha(2,3)-linked sialic acids on the cell surface to provide virion attachment to target cell. 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. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA.
Belongs to the polyomaviruses coat protein VP1 family.
Host nucleus
Blue Ice
+4°C
+4°C
This supplementary information is collated from multiple sources and compiled automatically.
The Polyomavirus strain RA Major Capsid VP1 is a structural protein essential for viral capsid formation often referred to simply as VP1. It has a molecular mass of approximately 42 kDa. This protein is a primary component of the virus's outer shell or capsid which encapsidates the viral DNA protecting it from degradation. Expression of VP1 occurs during the late phase of the polyomavirus lifecycle in infected host cells particularly within the nucleus where capsid assembly takes place.
Polyomavirus Major Capsid VP1 serves critical roles in virus assembly and host cell entry. As a principal capsid protein it associates with other capsid proteins VP2 and VP3 forming a complex important for virion structure. This complex facilitates the recognition and attachment to host cell receptors initiating viral entry via endocytosis. VP1's ability to self-assemble into capsids makes it a model for studying virus-like particle formation in various research contexts.
Major Capsid VP1 predominantly participates in the endocytosis pathway which enables the virus to infiltrate host cells. This infiltration relies on interaction with the host cell's surface gangliosides like GM1 a receptor in the endocytosis pathway facilitating transport to the endoplasmic reticulum for viral uncoating. VP1's involvement in this pathway intersects with cellular proteins such as clathrin vital for forming vesicles during endocytosis and trafficking within the cell.
Polyomavirus Major Capsid VP1 associates with diseases such as progressive multifocal leukoencephalopathy (PML) a demyelinating disease often seen in immunocompromised individuals. In PML the JC virus another member of the Polyomavirus family with a similar VP1 protein infects oligodendrocytes leading to neuronal damage. This capsid protein also relates to Merkel cell carcinoma where Merkel cell polyomavirus integrates into the host genome driving oncogenesis. VP1’s function connects with proteins involved in immune evasion contributing to disease progression and severity.
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SDS-PAGE showing ab74571 at approximately 43kDa (4.4μg/lane).Lane 1 represents the molecular weight ladder. From the bottom: 14.4, 18.4, 25.0, 35.0, 45.0, 66.2, 116.0 kDa.
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