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AB34749

Anti-Rubella Virus capsid antibody [9B11]

5

(3 Reviews)

|

(15 Publications)

Mouse Monoclonal POLS antibody. Suitable for WB, I-ELISA and reacts with Rubella virus samples. Cited in 15 publications.

View Alternative Names

Structural polyprotein, p110

1 Images
Western blot - Anti-Rubella Virus capsid antibody [9B11] (AB34749)
  • WB

Unknown

Western blot - Anti-Rubella Virus capsid antibody [9B11] (AB34749)

All lanes:

Western blot - Anti-Rubella Virus capsid antibody [9B11] (ab34749) at 1 µg/mL

Lane 1:

crude yeast cell lysate [mock control]

Lanes 2 - 3:

irrelevant viral proteins

Lane 4:

recombinant purified rubella capsid protein

Lane 5:

crude lysate of transformed yeast cells expressing rubella capsid protein

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

9B11

Isotype

IgG1

Carrier free

No

Reacts with

Rubella virus

Applications

I-ELISA, WB

applications

Reactivity data

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Product details

This product was changed from ascites to tissue culture supernatant on 28/11/2017. Lot numbers higher than GR120838-1 and GR210838-5 will be from tissue culture supernatant. Please note that the dilutions may need to be adjusted accordingly.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.1% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

The Rubella Virus capsid is an important structural component of the Rubella virus particle. Sometimes called the capsid protein or capsid proteins it is involved in the assembling and packaging of the viral genome into new virions. The Rubella Virus capsid protein is around 33 kilodaltons in mass. It is expressed within infected host cells where it facilitates the initial steps of viral replication and particle formation. This capsid protein is essential for the structural integrity of the virus ensuring proper encapsulation of the viral RNA.
Biological function summary

The Rubella Virus capsid interacts with various host cell factors to mediate processes like viral assembly and budding. It is part of a capsid protein complex which plays a role in the lifecycle of the virus by protecting the viral nucleic material. This nucleoprotein protein interacts with the host cell’s machinery influencing cell entry and immune evasion. The capsid elicits immune responses in the host which are detectable through assays such as the capsid ELISA often used in anti-rubella serological testing.

Pathways

The Rubella Virus capsid is closely associated with the viral replication pathway and immune signaling pathways. It partners with other viral proteins to regulate replication ensuring successful synthesis of new virus particles. The host immune response against the capsid is significant involving pathways that trigger antibody production. The interaction of capsid proteins with host elements can modify immune responses assisting the virus in evading detection. Notable related proteins include the envelope proteins which work in tandem during the viral lifecycle.

The Rubella Virus capsid is fundamentally linked to rubella particularly congenital rubella syndrome. This capsid protein triggers immune responses that may not fully prevent infection but are important in diagnostic evaluations through tools like anti-rubella ELISA. Rubella infection can impact fetal development during pregnancy leading to severe outcomes. The interaction of the capsid with other viral components like the nucleoprotein protein is significant in the spread and pathology of the virus influencing the course of infectivity and disease manifestation.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Capsid protein. Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter (PubMed : 28575072). The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes (PubMed : 28575072). Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion (PubMed : 24282305). Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32 (PubMed : 10823864). Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells (PubMed : 16051872). Induces apoptosis when expressed in transfected cells (PubMed : 11017784).. Spike glycoprotein E2. Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (PubMed : 28575072).. Spike glycoprotein E1. Class II viral fusion protein (PubMed : 23292515). Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (By similarity). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion (PubMed : 9765418). The cytoplasmic tail of spike glycoprotein E1 modulates virus release (PubMed : 10233921, PubMed : 10708417). The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (PubMed : 28575072).
See full target information Structural polyprotein

Additional targets

POLS_RUBVT

Publications (15)

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

International journal of molecular sciences 26: PubMed39940811

2025

Oxidative Stress Enhances Rubella Virus Infection in Immortalized Human First-Trimester Trophoblasts.

Applications

Unspecified application

Species

Unspecified reactive species

Quang Duy Trinh,Kazuhide Takada,Ngan Thi Kim Pham,Chika Takano,Takahiro Namiki,Shun Ito,Yoshinori Takeda,Shoko Okitsu,Hiroshi Ushijima,Satoshi Hayakawa,Shihoko Komine-Aizawa

eLife 12: PubMed37470786

2023

Rubella virus tropism and single-cell responses in human primary tissue and microglia-containing organoids.

Applications

Unspecified application

Species

Unspecified reactive species

Galina Popova,Hanna Retallack,Chang N Kim,Albert Wang,David Shin,Joseph L DeRisi,Tomasz Nowakowski

International journal of molecular sciences 23: PubMed36077193

2022

Rubella Virus Triggers Type I Interferon Antiviral Response in Cultured Human Neural Cells: Involvement in the Control of Viral Gene Expression and Infectious Progeny Production.

Applications

Unspecified application

Species

Unspecified reactive species

Sayuri Sakuragi,Huanan Liao,Kodai Yajima,Shigeyoshi Fujiwara,Hiroyuki Nakamura

Frontiers in microbiology 13:904189 PubMed35875557

2022

Enhancement of Rubella Virus Infection in Immortalized Human First-Trimester Trophoblasts Under Low-Glucose Stress Conditions.

Applications

Unspecified application

Species

Unspecified reactive species

Quang Duy Trinh,Kazuhide Takada,Ngan Thi Kim Pham,Chika Takano,Takahiro Namiki,Ryo Ikuta,Shingo Hayashida,Shoko Okitsu,Hiroshi Ushijima,Shihoko Komine-Aizawa,Satoshi Hayakawa

Viruses 14: PubMed35746641

2022

Low Susceptibility of Rubella Virus in First-Trimester Trophoblast Cell Lines.

Applications

Unspecified application

Species

Unspecified reactive species

Ngan Thi Kim Pham,Quang Duy Trinh,Kazuhide Takada,Shihoko Komine-Aizawa,Satoshi Hayakawa

Frontiers in immunology 12:796065 PubMed35003119

2021

Rubella Virus Infected Macrophages and Neutrophils Define Patterns of Granulomatous Inflammation in Inborn and Acquired Errors of Immunity.

Applications

Unspecified application

Species

Unspecified reactive species

Ludmila Perelygina,Raeesa Faisthalab,Emily Abernathy,Min-Hsin Chen,LiJuan Hao,Lionel Bercovitch,Diana K Bayer,Lenora M Noroski,Michael T Lam,Maria Pia Cicalese,Waleed Al-Herz,Arti Nanda,Joud Hajjar,Koen Vanden Driessche,Shari Schroven,Julie Leysen,Misha Rosenbach,Philipp Peters,Johannes Raedler,Michael H Albert,Roshini S Abraham,Hemalatha G Rangarjan,David Buchbinder,Lisa Kobrynski,Anne Pham-Huy,Julie Dhossche,Charlotte Cunningham Rundles,Anna K Meyer,Amy Theos,T Prescott Atkinson,Amy Musiek,Mehdi Adeli,Ute Derichs,Christoph Walz,Renate Krüger,Horst von Bernuth,Christoph Klein,Joseph Icenogle,Fabian Hauck,Kathleen E Sullivan

Microorganisms 9: PubMed33806778

2021

The Epithelial-to-Mesenchymal Transition-Like Process Induced by TGF-β1 Enhances Rubella Virus Binding and Infection in A549 Cells via the Smad Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Ngan Thi Kim Pham,Quang Duy Trinh,Kazuhide Takada,Chika Takano,Mari Sasano,Shoko Okitsu,Hiroshi Ushijima,Shihoko Komine-Aizawa,Satoshi Hayakawa

Genes to cells : devoted to molecular & cellular mechanisms 23:1023-1042 PubMed30318703

2018

Albatross/FBF1 contributes to both centriole duplication and centrosome separation.

Applications

Unspecified application

Species

Unspecified reactive species

Akihito Inoko,Tomoki Yano,Tatsuo Miyamoto,Shinya Matsuura,Tohru Kiyono,Naoki Goshima,Masaki Inagaki,Yuko Hayashi

IEEE journal of solid-state circuits 53:2054-2064 PubMed30559530

2018

High-Density Redox Amplified Coulostatic Discharge-Based Biosensor Array.

Applications

Unspecified application

Species

Unspecified reactive species

Alexander C Sun,Enrique Alvarez-Fontecilla,A G Venkatesh,Eliah Aronoff-Spencer,Drew A Hall

Viruses 10: PubMed29300335

2018

Myelin Oligodendrocyte Glycoprotein-Independent Rubella Infection of Keratinocytes and Resistance of First-Trimester Trophoblast Cells to Rubella Virus In Vitro.

Applications

Unspecified application

Species

Unspecified reactive species

Quang Duy Trinh,Ngan Thi Kim Pham,Kazuhide Takada,Shihoko Komine-Aizawa,Satoshi Hayakawa
View all publications

Product promise

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