Product Description
Size: 50µg
Recombinant JCV Polyomavirus Major Capsid VP1 protein is a JC polyomavirus Full Length protein, in the 1 to 354 aa range, expressed in Saccharomyces cerevisiae , with >95%, suitable for WB, SDS-PAGE.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Saccharomyces cerevisiae,
Tags:Tag free,
Applications:WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:JCV VP1 protein was purified and lyophilized assembled into virus like particles (VLPs). It is tested for hemagglutination activity and analysed using electron microscopy.,
Accession:P03089,
Animal free:No,
Carrier free:No,
Species:JC polyomavirus,
Reconstitution:Reconstitute in water,
Storage buffer:Constituents: PBS
Product details:
JCV VP1 protein was purified and lyophilized assembled into virus like particles (VLPs). It is tested for hemagglutination activity and analysed using electron microscopy.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The JCV Polyomavirus Major Capsid VP1 often referred to as JCV-VP1 is a protein essential for the structural integrity of the JC virus (JCV) a human polyomavirus. It weighs approximately 45 kDa and plays an important role in forming the viral capsid. The protein organizes into pentamers which assemble into the icosahedral shell of the virus. This major capsid protein is expressed in infected host cells where it facilitates the virus's ability to attach and enter host cells.
Biological function summary
The JCV-VP1 protein allows the JC virus to infect and replicate within human host cells. It forms a principal component of the viral capsid allowing the virus to protect its genetic material from the environment. This protein interacts with cell surface receptors on host cells which is important for the viral entry process. While VP1 is singularly integral to the capsid it operates alongside other proteins like VP2 and VP3 within the virus particle.
Pathways
The JCV-VP1 protein leverages host cellular pathways to support viral replication and spread. It ties into the endocytic pathway important for viral entry and interacts with major histocompatibility complex class I molecules like HLA-A*02:01. VP1 may engage with proteins involved in these pathways facilitating viral entry and consequent propagation within the host.
JCV-VP1 is significantly implicated in the development of Progressive Multifocal Leukoencephalopathy (PML) a neurological disorder occurring mostly in immunocompromised individuals. The protein's role in viral mechanisms makes it integral to the pathogenicity of the virus leading to PML. Additionally the Ri protein part of the human immune response may interact with VP1 as the body attempts to counteract JCV infection.
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Collaboration
Tony Tang
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