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AB20193

Anti-HSV1 ICP8 Major DNA binding protein antibody [10A3]

5

(1 Review)

|

(11 Publications)

Mouse Monoclonal DNBI antibody. Suitable for WB, ICC/IF and reacts with Herpes simplex virus, Purified native protein - Herpes simplex virus samples. Cited in 11 publications.

View Alternative Names

HSV1 DBP, Herpes simplex virus type 1 DBP, ICP8, Infected cell protein 8, Major DNA binding protein, UL29

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-HSV1 ICP8 Major DNA binding protein antibody [10A3] (AB20193)
  • ICC/IF

AbReview39584****

Immunocytochemistry/ Immunofluorescence - Anti-HSV1 ICP8 Major DNA binding protein antibody [10A3] (AB20193)

ab20193 staining HSV1 ICP8 Major DNA binding protein in Human U2OS by ICC/IF (Immunocytochemistry/immunofluorescence). Cells were fixed with paraformaldehyde, permeabilized with 0.5% Triton X-100 and blocked with 5% serum for 20 minutes at 22°C. Samples were incubated with primary antibody (1/100) for 1 hour at 22°C. An Alexa Fluor® 488-conjugated Goat anti-mouse IgG polyclonal (1/1000) was used as the secondary antibody.

This image is courtesy of an anonymous Abreview

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

10A3

Isotype

IgG1

Light chain type

unknown

Carrier free

No

Reacts with

Herpes simplex virus

Applications

WB, ICC/IF

applications

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Storage buffer
Preservative: 0.02% 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.

HSV1 ICP8 also known as the major DNA-binding protein is a vital component in the replication of herpes simplex virus type 1 (HSV1). Alternate names for this protein include infected cell protein 8 (ICP8) and 11E2. ICP8 boasts a molecular mass of approximately 128 kDa. This protein is expressed in HSV1-infected cells and exhibits strong DNA-binding properties. As a single-strand DNA-binding protein ICP8 facilitates the formation of complex viral replication machineries promoting helicase-primase activity necessary for viral DNA synthesis.
Biological function summary

ICP8 serves to orchestrate virus replication by acting at the core of the viral replication complex. It operates predominantly as a monomer but can form homo-oligomers in the presence of DNA. ICP8 interaction with other viral replication proteins such as UL5 UL52 and UL8 highlights its role as a scaffolding protein within the replication complex. Through binding and restructuring DNA ICP8 ensures efficient replication fork progression and genomic stability during HSV1 replication.

Pathways

ICP8 integrates critically into the replication pathway of HSV1. The replication process begins with initiation transitions through elongation and concludes with termination. Proteins related to these processes include UL9 which interacts with ICP8 to facilitate unwinding of the viral DNA. Another protein the polymerase-accessory protein UL42 works closely with ICP8 during the elongation of DNA synthesis. Through these interactions ICP8 plays a critical role in the orchestration and assembly of the HSV1 genome replication machinery.

ICP8 has a significant link to herpes simplex infections and diseases associated with viral latency and reactivation. HSV1 infections can lead to both oral herpes and more severe conditions such as herpes simplex encephalitis. The involvement of ICP8 extends to its interaction with cellular proteins that may affect immune evasion and viral persistence highlighting its potential importance in HSV1 pathogenesis. Understanding ICP8’s interaction with cellular proteins and its place in the disease cycle offers insight into therapeutic approaches targeting HSV1 infections.

Product protocols

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

Publications (11)

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

Proceedings of the National Academy of Sciences of the United States of America 118: PubMed34725147

2021

Preventing translational inhibition from ribosomal protein insufficiency by a herpes simplex virus-encoded ribosome-associated protein.

Applications

Unspecified application

Species

Unspecified reactive species

Elizabeth I Vink,John Andrews,Carol Duffy,Ian Mohr

Journal of virology 95:e0048621 PubMed33853961

2021

Herpes Simplex Virus 1 Coinfection Modifies Adeno-associated Virus Genome End Recombination.

Applications

Unspecified application

Species

Unspecified reactive species

Anita Felicitas Meier,Kurt Tobler,Kevin Michaelsen,Bernd Vogt,Els Henckaerts,Cornel Fraefel

PloS one 13:e0200955 PubMed30110337

2018

Herpes ICP8 protein stimulates homologous recombination in human cells.

Applications

Unspecified application

Species

Unspecified reactive species

Melvys Valledor,Richard S Myers,Paul C Schiller

Nature communications 9:1980 PubMed29773792

2018

MxB is an interferon-induced restriction factor of human herpesviruses.

Applications

Unspecified application

Species

Unspecified reactive species

Michel Crameri,Michael Bauer,Nicole Caduff,Raphael Walker,Fiona Steiner,Francesca D Franzoso,Cornelia Gujer,Karin Boucke,Talissa Kucera,Andrea Zbinden,Christian Münz,Cornel Fraefel,Urs F Greber,Jovan Pavlovic

Journal of virology 91: PubMed28515305

2017

Cell Cycle-Dependent Expression of Adeno-Associated Virus 2 (AAV2) Rep in Coinfections with Herpes Simplex Virus 1 (HSV-1) Gives Rise to a Mosaic of Cells Replicating either AAV2 or HSV-1.

Applications

Unspecified application

Species

Unspecified reactive species

Francesca D Franzoso,Michael Seyffert,Rebecca Vogel,Artur Yakimovich,Bruna de Andrade Pereira,Anita F Meier,Sereina O Sutter,Kurt Tobler,Bernd Vogt,Urs F Greber,Hildegard Büning,Mathias Ackermann,Cornel Fraefel

Journal of virology 86:143-55 PubMed22013059

2011

Adeno-associated virus type 2 modulates the host DNA damage response induced by herpes simplex virus 1 during coinfection.

Applications

Unspecified application

Species

Unspecified reactive species

Rebecca Vogel,Michael Seyffert,Regina Strasser,Anna P de Oliveira,Christiane Dresch,Daniel L Glauser,Nelly Jolinon,Anna Salvetti,Matthew D Weitzman,Mathias Ackermann,Cornel Fraefel

Antimicrobial agents and chemotherapy 55:3231-9 PubMed21576438

2011

Inhibition of herpes simplex virus type 1 and type 2 infections by peptide-derivatized dendrimers.

Applications

Unspecified application

Species

Unspecified reactive species

Anna Luganini,Silvia Fabiole Nicoletto,Lorena Pizzuto,Giovanna Pirri,Andrea Giuliani,Santo Landolfo,Giorgio Gribaudo

Journal of virology 84:3808-24 PubMed20106923

2010

Inhibition of herpes simplex virus type 1 replication by adeno-associated virus rep proteins depends on their combined DNA-binding and ATPase/helicase activities.

Applications

WB, ICC/IF

Species

Unspecified reactive species, Unspecified reactive species

Daniel L Glauser,Michael Seyffert,Regina Strasser,Marco Franchini,Andrea S Laimbacher,Christiane Dresch,Anna Paula de Oliveira,Rebecca Vogel,Hildegard Büning,Anna Salvetti,Mathias Ackermann,Cornel Fraefel

Journal of virology 83:5309-20 PubMed19321610

2009

Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication.

Applications

WB

Species

Unspecified reactive species

Stuart K Souki,Paul D Gershon,Rozanne M Sandri-Goldin

Journal of virology 82:4974-90 PubMed18337577

2008

Live visualization of herpes simplex virus type 1 compartment dynamics.

Applications

WB

Species

Unspecified reactive species

Anna Paula de Oliveira,Daniel L Glauser,Andrea S Laimbacher,Regina Strasser,Elisabeth M Schraner,Peter Wild,Urs Ziegler,Xandra O Breakefield,Mathias Ackermann,Cornel Fraefel
View all publications

Product promise

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