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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% purity and suitable for ELISA, WB, SDS-PAGE.

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Images

SDS-PAGE - Recombinant Polyomavirus strain RA Major Capsid VP1 protein (AB74571), expandable thumbnail

Key facts

Purity

>75% SDS-PAGE

Expression system

Saccharomyces cerevisiae

Tags

Tag free

Applications

ELISA, WB, SDS-PAGE

Biologically active

No

Reactivity data

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

-

Target data

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.

Targets

Polyomavirus strain RA Major Capsid VP1

Alternative names

Recommended products

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.

Key facts

Purity

>75% SDS-PAGE

Expression system

Saccharomyces cerevisiae

Applications

ELISA, WB, SDS-PAGE

Accession
P03090-1
Animal free

No

Species

Murine polyomavirus strain A2

Reconstitution

Reconstitute in water

Concentration
Loading...
Storage buffer

Constituents: PBS

Sequence info

Amino acid sequence

Accession

P03090

Protein length

Full Length

Nature

Recombinant

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

Storage

Shipped at conditions

Blue Ice

Appropriate short-term storage conditions

+4°C

Appropriate long-term storage conditions

+4°C

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

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.

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.

Associated diseases and disorders

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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1 product image

  • SDS-PAGE - Recombinant Polyomavirus strain RA Major Capsid VP1 protein (ab74571), expandable thumbnail

    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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