Recombinant Polyomavirus strain RA Major Capsid VP1 protein
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Recombinant Polyomavirus strain RA Major Capsid VP1 protein is a Murine polyomavirus strain A2 Full Length protein, expressed in Saccharomyces cerevisiae , with >75%, suitable for ELISA, WB, SDS-PAGE.
View Alternative Names
Major capsid protein VP1, Major structural protein VP1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Polyomavirus strain RA Major Capsid VP1 protein (AB74571)
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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Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Lyophilized
Additional notes
Purified by ultracentifugation
General info
Function
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.
Sequence similarities
Belongs to the polyomaviruses coat protein VP1 family.
Subcellular localisation
Host nucleus
Target data
Product promise
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