JCV Polyomavirus Major Capsid VP1 full length protein (ab74569)

Overview

  • Product nameJCV Polyomavirus Major Capsid VP1 full length protein
  • DescriptionJCV Polyomavirus Major Capsid VP1 full length protein

Description

  • NatureRecombinant
  • SourceSaccharomyces cerevisiae
  • Amino Acid Sequence
    • Amino acids0 to 0

Specifications

Our Abpromise guarantee covers the use of ab74569 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    ELISA

    Western blot

    SDS-PAGE

  • Purity> 95 % by SDS-PAGE.
    Purified by ultracentifugation.
  • FormLyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Store at +4°C.

    Preservative: None
    Constituents: PBS

  • ReconstitutionReconstitute with deionized H2O. After reconstitution store at 4°C.

General info

  • Alternative names
    • Capsid protein VP1
  • RelevanceThe human polyomavirus JC virus (JCV) infects greater than 80% of the human population. The JC virus is a small (38-40 nm in diameter) double stranded, circular DNA virus covered by an icosahedral capsid. Infection with JCV is asymptomatic and it occurs in early childhood. After the primary infection, the virus remains in latent state in the kidney, until it's reactivation under immunosuppressive conditions to result in Progressive Multifocal Leukoencephalopathy (PML), a fatal demyelinating disease. 70% of all HIV-1- infected patients will exhibit neurological disorders and between 5 and 8% of all HIV-1-infected patients will develop PML. Similar to other polyomaviruses, JCV can cause tumors when intracerebrally inoculated at high titers into developing rodent. Several reports suggest the association of viruses, especially of the polyomavirus family with different types of human brain tumors. Tumorigenecity of JCV is most likely induced by the viral early gene product T-antigen. T-antigen has the capacity to interact with several tumor suppressor proteins, most notably p53, and functionally inactivate these proteins.
  • Cellular localizationVirion. Nucleus

JCV Polyomavirus Major Capsid VP1 full length protein images

  • SDS-PAGE showing ab74569 (4µg/lane).
    Lane 1 reprents the molecular weight ladder. From the bottom: 14.4, 18.4, 25.0, 35.0, 45.0, 66.2 kDa

References for JCV Polyomavirus Major Capsid VP1 full length protein (ab74569)

ab74569 has not yet been referenced specifically in any publications.

Product Wall

In regards to the JCV VP1 Protein, ab74569. JCV Polyomavirus Major Capsid VP1 protein is supplied in the form of VLP (Virus-like particles). Actually it is a higher structure formed from pentamers, but not pentamers itself.

Thank you for contacting us.



JCV VP1 was purified assembled into virus like particles (VLPs).

VLP is the structure formed from pentamers, but in fact it is not pentamer or monomer form of VP1.

I hope this info...

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We have been informed by the lab that JCV VP1 was purified and lyophilized assembled into virus like particles (VLPs). VLP structure is formed from pentamers, but in fact it is not pentamer or monomer form of VP1.



Die Spezifitätsnotiz beschreibt folgendes:

ab34756 bindet das Major Capsidprotein VP1 von humanem Polyoma Virus JCV und das Capsidprotein VP1 von hamster polyomavirus (HaPyV) and Simian Virus 40 (SV40).

ab34756 kreuz-...

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Thank you for your reply. I can confirm that the antibody ab34756 will react with the SV40 VP1 protein ab74565. On the antibody datasheet in the section labelled "cross-reactivity", it notes that it does react with the VP1 protein of SV40. I hope this...

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Thank you for your call this week and for your patience while I have been in touch with the production lab about these proteins. I have confirmed with the lab that these proteins do not contain any tag. To detect them, you could use specific monoclonal...

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"