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AB19311

Anti-UL42 antibody [2H4]

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(7 Publications)

Mouse Monoclonal PAP antibody. Suitable for IP, ELISA, WB, ICC/IF, IHC-Fr and reacts with Herpes simplex virus samples. Cited in 7 publications.

View Alternative Names

HHV1gp061

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

2H4

Isotype

IgG1

Carrier free

No

Reacts with

Herpes simplex virus

Applications

ELISA, WB, IP, IHC-Fr, ICC/IF

applications

Specificity

2H4 will recognise UL42 bound to HSV polymerase.

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.

UL42 also known as UL42 processivity factor is a DNA polymerase accessory protein found in herpes simplex virus (HSV). It plays an important role in the replication of viral DNA by binding to the DNA polymerase. UL42 has a molecular weight of approximately 65 kilodaltons and expresses in infected cells during the lytic cycle. Its primary function is to increase the processivity of the DNA polymerase enzyme allowing for efficient viral DNA synthesis. UL42 achieves this by attaching tightly to the DNA providing a clamp-like function for the polymerase.
Biological function summary

The UL42 protein interacts with the HSV DNA polymerase to form a complex critical for replication. The complex stabilizes the polymerase-DNA interaction significantly enhancing the polymerase's ability to synthesize long strands of DNA without detaching. The persistence of the complex is essential for continuous and efficient viral replication which is an important aspect of the herpes virus's ability to maintain infection in the host.

Pathways

The role of UL42 in DNA replication situates it within the viral replication pathways. It specifically contributes to the HSV lifecycle by ensuring the viral genome is copied efficiently. UL42 interacts particularly with the UL30 protein the catalytic subunit of the viral DNA polymerase. This interaction is important within the replication fork structure which is a significant aspect of HSV-specific viral replication pathways. The concerted action of UL42 and UL30 ensures that the viral DNA synthesis process is completed successfully.

UL42 is closely related to herpes simplex infections which can lead to conditions such as cold sores and genital herpes. The efficiency of viral replication driven by the UL42 and UL30 complex plays a direct role in disease progression and symptom manifestation. Understanding the function of UL42 can aid in developing targeted therapies which aim to disrupt this interaction and consequently reduce viral replication and disease severity.

Product protocols

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

Publications (7)

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

Biotechnology and bioengineering 122:424-434 PubMed39578398

2024

Expression of Viral DNA Polymerase in Synthetic Recombinant Adeno-Associated Virus Producer Cell Line Enhances Full Particle Productivity.

Applications

Unspecified application

Species

Unspecified reactive species

Yu-Chieh Lin,Han-Jung Kuo,Min Lu,Carissa Rungkittikhun,Wei-Shou Hu

Frontiers in microbiology 12:797279 PubMed35185822

2022

Hsp90 Inhibitors Prevent HSV-1 Replication by Directly Targeting UL42-Hsp90 Complex.

Applications

Unspecified application

Species

Unspecified reactive species

Shurong Qin,Xiao Hu,Shimin Lin,Ji Xiao,Zhaoyang Wang,Jiaoyan Jia,Xiaowei Song,Kaisheng Liu,Zhe Ren,Yifei Wang

Journal of virology 94: PubMed32699090

2020

Antiviral Properties of the LSD1 Inhibitor SP-2509.

Applications

Unspecified application

Species

Unspecified reactive species

Mitchell R Harancher,Jessica E Packard,Shane P Cowan,Neal A DeLuca,Jill A Dembowski

Antiviral research 159:55-62 PubMed30266338

2018

Ivermectin inhibits DNA polymerase UL42 of pseudorabies virus entrance into the nucleus and proliferation of the virus in vitro and vivo.

Applications

Unspecified application

Species

Unspecified reactive species

Changjie Lv,Wenkai Liu,Bin Wang,Ruyi Dang,Li Qiu,Juan Ren,Chuanqi Yan,Zengqi Yang,Xinglong Wang

PLoS pathogens 14:e1006823 PubMed29304174

2018

Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.

Applications

Unspecified application

Species

Unspecified reactive species

Katinka Döhner,Ana Ramos-Nascimento,Dagmara Bialy,Fenja Anderson,Ana Hickford-Martinez,Franziska Rother,Thalea Koithan,Kathrin Rudolph,Anna Buch,Ute Prank,Anne Binz,Stefanie Hügel,Robert Jan Lebbink,Rob C Hoeben,Enno Hartmann,Michael Bader,Rudolf Bauerfeind,Beate Sodeik

PLoS pathogens 13:e1006166 PubMed28095497

2017

Replication-Coupled Recruitment of Viral and Cellular Factors to Herpes Simplex Virus Type 1 Replication Forks for the Maintenance and Expression of Viral Genomes.

Applications

Unspecified application

Species

Unspecified reactive species

Jill A Dembowski,Sarah E Dremel,Neal A DeLuca

Journal of virology 81:8742-51 PubMed17553899

2007

A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.

Applications

ICC/IF, WB

Species

Unspecified reactive species, Unspecified reactive species

Yan Chen,Christine M Livingston,Stacy D Carrington-Lawrence,Ping Bai,Sandra K Weller
View all publications

Product promise

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