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AB123995

Native Adenovirus Type 5 hexon protein

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(3 Publications)

Native Adenovirus Type 5 hexon protein is a Human adenovirus 5 Full Length protein, in the 2 to 952 aa range, expressed in Native, with >95%, suitable for SDS-PAGE, ELISA.

View Alternative Names

Hexon protein, CP-H, Protein II, L3

1 Images
SDS-PAGE - Native Adenovirus Type 5 hexon protein (AB123995)
  • SDS-PAGE

Unknown

SDS-PAGE - Native Adenovirus Type 5 hexon protein (AB123995)

Lane 1 : Ladder
Lane 2 : Ad5
Lane 3 : Ad5 crude prep
Lane 4 : Ad5 prep after filtration
Lane 5 : Hybrid purified Hexon

Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Tags

Tag free

Applications

ELISA, SDS-PAGE

applications

Biologically active

No

Accession

P04133

Animal free

No

Carrier free

No

Species

Human adenovirus 5

Storage buffer

pH: 7 - 8 Preservative: 0.09% Sodium azide Constituents: 2.19% Sodium chloride, 0.28% Bis-Tris propane

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Hexon protein naturally self assembles as part of the virus life cycle. When the protein is purified we also see evidence of self assembly such as rapid loss of protein upon serial dilution. The storage buffer and ELISA coating buffer play an important role in the likelihood of self assembly and thereby can affect results when using purified hexon as antigen in ELISAs and other such assays. Many common ELISA coating buffers increase self assembly in hexon protein as they are designed to increase efficiency of antigen adsorption. This results in a very high signal with the initial dilution but then the sensitivity tails off very rapidly. Diluting and coating the hexon in water alone slightly increases sensitivity but reduces strength; coating and diluting in the presence of a small amount of stabilising protein (such as BSA) seems to increase sensitivity for antigen coating significantly (although too much BSA can block high concentrations of hexon).

This protein is derived from a pathogenic organism, and may be involved in a disease process, consequently exposure may have adverse health effects.

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"108 kDa","actualMolecularWeight":null,"aminoAcidEnd":952,"aminoAcidStart":2,"nature":"Native","expressionSystem":null,"accessionNumber":"P04133","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The Adenovirus Type 5 hexon also known as hexon protein or 5 protein is a major structural component of adenovirus capsid with a mass of approximately 960 kDa. Hexon proteins form the outer shell of the virus giving it stability and shape. These proteins are heavily expressed on the surface of human adenovirus serotype 5 a common virus strain used in therapeutic vector development. Hexon comprises three regions: the hypervariable regions conserved regions and the base that interacts with other capsid proteins.
Biological function summary

Adenovirus hexon proteins participate in the assembly and stability of the virus capsid complex. The hexon proteins interact with other components like penton base and fiber proteins to form a robust and protective viral coat. Their function involves binding to cell surface receptors such as the coxsackievirus and adenovirus receptor (CAR) allowing the virus to attach to and enter host cells. This interaction is key in viral infections and also in viral vector efficiency.

Pathways

The adenovirus Type 5 hexon protein plays important roles in immune evasion and viral entry pathways. The hexon protein helps the virus escape host immune detection by eluding neutralizing antibodies. The internal pathways also involve interactions with proteins like E1A which modulates host cell cycle pathways for viral replication. These interactions integrate hexon proteins into the broader adenoviral life cycle and infection processes.

Infections involving adenovirus Type 5 relate to respiratory illnesses and conjunctivitis. Respiratory infections often occur in crowded environments such as schools and military barracks and the hexon protein's interaction with the immune system can exacerbate symptoms. Additionally due to its prevalent role in viral vector design research on hexon relates to gene therapy contexts scrutinizing how hexon modifications impact disease treatment and host immune response. Hemagglutinin might connect to respiratory disorders linked to adenovirus making it also relevant in developing therapies.

Specifications

Form

Liquid

Additional notes

Purification involves multiple steps including sequential size exclusion and ion exchange chromatography.

General info

Function

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.

Sequence similarities

Belongs to the adenoviridae hexon protein family.

Subcellular localisation

Host nucleus

Product protocols

Target data

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.
See full target information L3

Publications (3)

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

Blood advances 8:5880-5884 PubMed39058975

2024

Coordinated antiviral immune response in a patient with myeloma and systemic adenovirus infection post-BCMA CAR T cells.

Applications

Unspecified application

Species

Unspecified reactive species

Mehmet H Kocoglu,Tim Luetkens,Jacqueline T Bork,John Baddley,Destiny Omili,Etse Gebru,Rediet Mulatu,Daniel Yamoah,Thierry Iraguha,Xiaoxuan Fan,Patricia Lesho,Mohammad Yousaf,Jillian M Baker,Kenneth A Dietze,Kim G Hankey,Ashraf Badros,Jean A Yared,Aaron P Rapoport,Nancy M Hardy,Djordje Atanackovic

Science immunology 6:eabi8635 PubMed34648369

2021

Fractionating a COVID-19 Ad5-vectored vaccine improves virus-specific immunity.

Applications

Unspecified application

Species

Unspecified reactive species

Sarah Sanchez,Nicole Palacio,Tanushree Dangi,Thomas Ciucci,Pablo Penaloza-MacMaster

Journal of virology 87:1893-8 PubMed23175361

2012

Amino acid exchanges in the putative nuclear export signal of adenovirus type 5 L4-100K severely reduce viral progeny due to effects on hexon biogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Orkide O Koyuncu,Thomas Speiseder,Thomas Dobner,Melanie Schmid
View all publications

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