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AB43812

Anti-Respiratory Syncytial Virus antibody [2F7]

5

(1 Review)

|

(28 Publications)

Anti-Respiratory Syncytial Virus antibody [2F7] (ab43812) is a mouse monoclonal antibody detecting Respiratory Syncytial Virus in Western Blot, IHC-Fr, ICC/IF, ELISA. Suitable for Respiratory syncytial virus.

- Over 10 publications
- Trusted since 2006

View Alternative Names

Fusion glycoprotein F0, F

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-Respiratory Syncytial Virus antibody [2F7] (AB43812)
  • ICC/IF

PubMed

Immunocytochemistry/ Immunofluorescence - Anti-Respiratory Syncytial Virus antibody [2F7] (AB43812)

Immunofluorescent staining of Respiratory Syncytial Virus F protein Bound to HeLa cells using ab43812. Respiratory Syncytial Virus F protein was visualized in green and Respiratory Syncytial N protein in red.

Image from Krzyzaniak MA et al., PLoS Pathogens. 2013;9(4):e1003309. Fig 2.; doi: 10.1371/journal.ppat.1003309 Reproduced under the Creative Commons license http://creativecommons.org/licenses/by/4.0/

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

2F7

Isotype

IgG1

Light chain type

kappa

Carrier free

No

Reacts with

Respiratory syncytial virus

Applications

IHC-Fr, ICC/IF, WB, ELISA

applications

Reactivity data

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Product details

What is this antibody validated in?
Anti-Respiratory Syncytial Virus antibody [2F7] (ab43812) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunohistochemistry (IHC-Fr), Immunocytochemistry/immunofluorescence (ICC/IF), ELISA in Respiratory syncytial virus samples.

What is the molecular weight of Respiratory Syncytial Virus?
Anti-Respiratory Syncytial Virus [2F7] (ab43812) specifically detects a band for Respiratory Syncytial Virus (UniProt: P03420) at a molecular weight of 48 , 70kDa.

Trusted by the scientific community
Anti-Respiratory Syncytial Virus [2F7] (ab43812) was first used in a scientific publication in 2006 and has been cited over 10 times in peer-reviewed journals.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Constituents: 2% Sucrose, 1.21% Tris, 0.75% Glycine
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.

Respiratory Syncytial Virus (RSV) is a negative-sense single-stranded RNA virus known to cause respiratory infections. It belongs to the Paramyxoviridae family and is sometimes referred to by its alternate names like Human Orthopneumovirus. RSV is approximately 15 kb in size. It is predominantly expressed in the respiratory tract where it attacks epithelial cells leading to infection. The virus's ability to form a syncytium a large multinucleate cell is one of its mechanical strategies to aid in the spread across the host cells.
Biological function summary

The virus propagates efficiently within the host tissue leading to serious respiratory illness in infants and young children. RSV is not part of a specific complex but it engages host cellular machinery to promote its replication and prevent immune detection. The fusion (F) protein of RSV plays a critical role in mediating membrane fusion facilitating viral entry into the host cells. The involvement of viral proteins in modulating host immune responses is significant for the virus's life cycle.

Pathways

Respiratory infections caused by RSV connect to the host's immune signaling pathways including the toll-like receptor (TLR) pathways and the interferon response pathway. The interaction of RSV proteins with these pathways leads to an increased inflammatory response. Proteins such as the RSV G protein interface with the chemokine receptor pathway which helps in modulation of the immune system to allow viral persistence. These interactions demonstrate the virus's strategies to evade immune surveillance and promote infection.

Respiratory syncytial virus is a major cause of bronchiolitis and pneumonia in infants and young children. The virus's activity in the respiratory tract contributes to severe inflammation and cell damage which can lead to hospitalization. Other proteins like RSV M protein are involved in virus assembly and budding and they passively influence disease progression by impacting viral load and the host's immune response. Understanding these interactions is important for developing therapeutic strategies including anti-RSV monoclonal antibodies like palivizumab (2F7) which target prominent viral components to prevent severe disease outcomes.

Product protocols

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

Target data

Fusion glycoprotein F0. Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.. Fusion glycoprotein F1. Class I viral fusion protein (PubMed : 23618766). Under the current model, the protein has at least 3 conformational states : pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state (PubMed : 23618766). During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain (PubMed : 19966279, PubMed : 23618766). The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm (PubMed : 23593008, PubMed : 23618766). This fusion is pH independent and occurs at the plasma or endosomal membrane (Probable). The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed : 10864656). F protein is involved in the entry into the host cell through the interaction with host IGF1R (PubMed : 32494007). This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed : 21841784, PubMed : 32494007). Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed : 10438814). F protein may trigger p53-dependent apoptosis (PubMed : 18216092).. Fusion glycoprotein F2. Major determinant of the species specificity of RSV infection (PubMed : 12663767). The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed : 10864656). F protein is involved in the entry into the host cell through the interaction with host IGF1R (PubMed : 32494007). This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed : 32494007). Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed : 10438814). F protein seems to trigger p53-dependent apoptosis (PubMed : 18216092).
See full target information F

Publications (28)

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

Viruses 17: PubMed40733508

2025

Broad-Spectrum Antiviral Activity of Pyridobenzothiazolone Analogues Against Respiratory Viruses.

Applications

Unspecified application

Species

Unspecified reactive species

Elisa Feyles,Tommaso Felicetti,Irene Arduino,Massimo Rittà,Andrea Civra,Luisa Muratori,Stefania Raimondo,David Lembo,Giuseppe Manfroni,Manuela Donalisio

Scientific reports 15:19708 PubMed40467662

2025

Plasmonic optical fiber biosensors for ultra-low detection of respiratory syncytial virus via point-of-care tests.

Applications

Unspecified application

Species

Unspecified reactive species

Federica Passeggio,Luigi Zeni,Massimiliano Galdiero,Francesco Arcadio,Carla Zannella,Anna De Filippis,Chiara Marzano,Ines Tavoletta,Fabiana Napolitano,Rosalba Pitruzzella,Giuseppe Portella,Nunzio Cennamo

Viruses 16: PubMed39772190

2025

Interaction Between the Matrix Protein and the Polymerase Complex of Respiratory Syncytial Virus.

Applications

Unspecified application

Species

Unspecified reactive species

Elliot B Atchison,Sarah N Croft,Cynthia Mathew,Daniel W Brookes,Matthew Coates,Kazuhiro Ito,Reena Ghildyal

Frontiers in cellular and infection microbiology 14:1484245 PubMed39776441

2025

Fumarprotocetraric acid and geraniin were identified as novel inhibitors of human respiratory syncytial virus infection .

Applications

Unspecified application

Species

Unspecified reactive species

Chao Wang,Yi-Man Huang,Jun Zhao,Yi-Ming Bai,Cai-Qin Yan,Guan-Hua Du,Li-Shu Zheng,Ai-Lin Liu

PLoS pathogens 20:e1012687 PubMed39561185

2024

Antagonism of BST2/Tetherin, a new restriction factor of respiratory syncytial virus, requires the viral NS1 protein.

Applications

Unspecified application

Species

Unspecified reactive species

Katherine Marougka,Delphine Judith,Tristan Jaouen,Sabine Blouquit-Laye,Gina Cosentino,Clarisse Berlioz-Torrent,Marie-Anne Rameix-Welti,Delphine Sitterlin

Viruses 16: PubMed38932114

2024

Respiratory Syncytial Virus Vaccine Design Using Structure-Based Machine-Learning Models.

Applications

Unspecified application

Species

Unspecified reactive species

Thomas C McCarty,Iosif I Vaisman

Signal transduction and targeted therapy 9:144 PubMed38853183

2024

Farnesyltransferase inhibitor lonafarnib suppresses respiratory syncytial virus infection by blocking conformational change of fusion glycoprotein.

Applications

Unspecified application

Species

Unspecified reactive species

Qi Yang,Bao Xue,Fengjiang Liu,Yongzhi Lu,Jielin Tang,Mengrong Yan,Qiong Wu,Ruyi Chen,Anqi Zhou,Lijie Liu,Junjun Liu,Changbin Qu,Qingxin Wu,Muqing Fu,Jiayi Zhong,Jianwei Dong,Sijie Chen,Fan Wang,Yuan Zhou,Jie Zheng,Wei Peng,Jinsai Shang,Xinwen Chen

PLoS pathogens 20:e1012198 PubMed38739647

2024

Intranasal respiratory syncytial virus vaccine attenuated by codon-pair deoptimization of seven open reading frames is genetically stable and elicits mucosal and systemic immunity and protection against challenge virus replication in hamsters.

Applications

Unspecified application

Species

Unspecified reactive species

Megan Levy,Jessica W Chen,Jaclyn A Kaiser,Hong-Su Park,Xueqiao Liu,Lijuan Yang,Celia Santos,Ursula J Buchholz,Cyril Le Nouën

Science signaling 16:eabq1173 PubMed38085817

2023

Nonself RNA rewires IFN-β signaling: A mathematical model of the innate immune response.

Applications

Unspecified application

Species

Unspecified reactive species

Zbigniew Korwek,Maciej Czerkies,Joanna Jaruszewicz-Błońska,Wiktor Prus,Ilona Kosiuk,Marek Kochańczyk,Tomasz Lipniacki

PLoS pathogens 19:e1011597 PubMed37669278

2023

Antagonism between viral infection and innate immunity at the single-cell level.

Applications

Unspecified application

Species

Unspecified reactive species

Frederic Grabowski,Marek Kochańczyk,Zbigniew Korwek,Maciej Czerkies,Wiktor Prus,Tomasz Lipniacki
View all publications

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