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AB74569

重组JCV Polyomavirus Major Capsid VP1蛋白

Recombinant JCV Polyomavirus Major Capsid VP1 protein

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(4 Publications)

Recombinant JCV Polyomavirus Major Capsid VP1 protein is a Full Length protein, in the 1 to 354 aa range, expressed in Saccharomyces cerevisiae , with >95%, suitable for WB, SDS-PAGE, FuncS.
3 Images
Western blot - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)
  • WB

Supplier Data

Western blot - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)

Western blot showing ab74569 (Lane 1) MW ladder (Lane 2)

All lanes:

Western blot - Recombinant JCV Polyomavirus Major Capsid VP1 protein (ab74569)

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SDS-PAGE - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)

SDS-PAGE showing ab74569 (Lane 1)
Lane 2 reprents the molecular weight ladder.

SDS-PAGE - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant JCV Polyomavirus Major Capsid VP1 protein (AB74569)

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

关键信息

纯度

>95% SDS-PAGE

表达系统

Saccharomyces cerevisiae

标签

Tag free

应用

WB, FuncS, SDS-PAGE

applications

生物活性

Yes

生物学活性

JCV VP1 protein was purified and lyophilized assembled into virus like particles (VLPs). It is tested for hemagglutination activity and analysed using electron microscopy.

不含动物源

No

不含载体蛋白

No

复溶

Reconstitute in water

存储溶液

Constituents: PBS

storage-buffer

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反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1 µg/mL", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"4 µg/mL", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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产品详情

JCV VP1 protein was purified and lyophilized assembled into virus like particles (VLPs). It is tested for hemagglutination activity and analysed using electron microscopy.
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序列信息

[{"sequence":"MAPTKRKGERKDPVQVPKLLIRGGVEVLEVKTGVDSITEVECFLTPEMGDPDEHLRGFSKSISISDTFESDSPNKDMLPCYSVARIPLPNLNEDLTCGNILMWEAVTLKTEVLGVTTLMNVHSNGQATHDNGAGKPVQGTSFHFFSVGGEALELQGVVFNYRTKYPDGTIFPKNATVQSQVMNTEHKAYLDKNKAYPVECWVPDPTRNENTRYFGTLTGGENVPPVLHITNTATTVLLDEFGVGPLCKGDNLYLSAVDVCGMFTNRSGSQQWRGLSRYFKVQLRKRRVKNPYPISFLLTDLINRRTPRVDGQPMYGMDAQIEEVRVFEGTEELPGDPDMMRYVDRYGQLQTKML","proteinLength":"Full Length","predictedMolecularWeight":"39.6 kDa","actualMolecularWeight":"41 kDa","aminoAcidEnd":354,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Saccharomyces cerevisiae ","accessionNumber":null,"tags":[]}]
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性能和储存信息

运输条件
Blue Ice
推荐的短期储存条件
+4°C
推荐的长期储存条件
+4°C
True
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补充信息

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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特殊说明

形式

Lyophilized

附加说明

Purified by ultracentifugation.

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常规信息

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产品实验方案

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靶点信息

See full target information VP1_POVJC
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文献 (4)

Recent publications for all applications. Explore the full list and refine your search

The Journal of infectious diseases 229:1836-1844 PubMed37774496

2023

Upregulation of the NKG2D Ligand ULBP2 by JC Polyomavirus Infection Promotes Immune Recognition by Natural Killer Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Stephanie Jost,Jenny Ahn,Sarah Chen,Taylor Yoder,Kayitare Eunice Gikundiro,Esther Lee,Simon B Gressens,Kyle Kroll,Melissa Craemer,G Campbell Kaynor,Michelle Lifton,C Sabrina Tan

Journal of acquired immune deficiency syndromes (1999) 82:220-224 PubMed31513076

2019

Brief Report: Decreased JC Virus-Specific Antibody-Dependent Cellular Cytotoxicity in HIV-Seropositive PML Survivors.

Applications

Unspecified application

Species

Unspecified reactive species

Chen S Tan,Joshua Ghofrani,Emma Geiger,Igor J Koralnik,Stephanie Jost

Genes 10: PubMed30736350

2019

Nucleolar Expression and Chromosomal Associations in Robertsonian Spermatocytes of .

Applications

Unspecified application

Species

Unspecified reactive species

Fernanda López-Moncada,Daniel Tapia,Nolberto Zuñiga,Eliana Ayarza,Julio López-Fenner,Carlo Alberto Redi,Soledad Berríos

Biotechnology progress 30:744-8 PubMed24574306

2014

Effect of the DnaK chaperone on the conformational quality of JCV VP1 virus-like particles produced in Escherichia coli.

Applications

Unspecified application

Species

Unspecified reactive species

Paolo Saccardo,Escarlata Rodríguez-Carmona,Antonio Villaverde,Neus Ferrer-Miralles
View all publications
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