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AB6506

Anti-HSV1 + HSV2 gB antibody [10B7]

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(44 Publications)

Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) is a mouse monoclonal antibody detecting HSV1 + HSV2 gB in Western Blot, ICC/IF. Suitable for Herpes simplex virus, Human herpesvirus 2.

- Over 30 publications
- Trusted since 2001

View Alternative Names

UL27, gB, Envelope glycoprotein B

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-HSV1 + HSV2 gB antibody [10B7] (AB6506)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-HSV1 + HSV2 gB antibody [10B7] (AB6506)

Green : immunofluorescence staining of HSV1 or HSV2 of Vero (African green monkey) cells ( HSV-1 is strain MacIntyre, HSV-2 is strain G) on slides, using ab6506 (1 : 100) (secondary anti-mouse-FITC). Red : counterstain in the conjugate preparation.

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (AB6506)
  • WB

Unknown

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (AB6506)

Lanes 1 and 8:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/1600 dilution

Lane 2:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/3200 dilution

Lane 3:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/6400 dilution

Lane 4:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/12800 dilution

Lane 5:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/200 dilution

Lane 6:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/400 dilution

Lane 7:

Western blot - Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) at 1/800 dilution

Lanes 1 - 4:

Vero cells infected with HSV1

Lanes 5 - 8:

Vero cells infected with HSV2

false

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

10B7

Isotype

IgG1

Light chain type

kappa

Carrier free

Yes

Reacts with

Herpes simplex virus, Human herpesvirus 2

Applications

WB, ICC/IF

applications

Reactivity data

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Product details

What is this antibody validated in?
Anti-HSV1 + HSV2 gB antibody [10B7] (ab6506) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunocytochemistry/immunofluorescence (ICC/IF) in Herpes simplex virus, Human herpesvirus 2 samples.

Trusted by the scientific community
Anti-HSV1 + HSV2 gB [10B7] (ab6506) was first used in a scientific publication in 2001 and has been cited over 30 times in peer-reviewed journals.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

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

The glycoprotein B (gB) of Herpes Simplex Virus type 1 (HSV1) and type 2 (HSV2) is an important viral protein responsible for membrane fusion during viral entry and cell-to-cell spread. This protein is referred to as gB in both HSV1 and HSV2 contexts. Glycoprotein B has an approximate molecular mass of 110 kDa and is expressed on the surface of the viral envelope. It is highly conserved across alpha-herpesviruses. HSV1 and HSV2 gB play critical roles in the herpesvirus infection cycle facilitating the virus's ability to infect cells and spread within the host.
Biological function summary

Glycoprotein B facilitates the fusion of the viral envelope with the host cell membrane which is essential for viral entry. gB functions as part of a complex with other glycoproteins particularly gD gH and gL to mediate this fusion process. The interaction between gB and these glycoproteins is important for the virus to penetrate host cells. The conserved structure of gB allows it to participate in membrane fusion events that enable the virus to escape immune detection and maintain infection in the host.

Pathways

Glycoprotein B of HSV1 and HSV2 interacts with cellular signaling pathways that influence viral entry and immune evasion. gB is a part of the fusion machinery essential for the fusion pathway working closely with other fusion-associated proteins such as gH and gL. It is integrated into the herpesvirus life cycle including viral replication and spread. The interaction of gB with cellular receptors on the host cell membrane exemplifies its role in co-opting host cellular mechanisms to facilitate viral transmission and infection.

HSV1 and HSV2 gB is associated with herpes simplex infections leading to conditions like oral herpes (HSV1) and genital herpes (HSV2). Glycoprotein B's role in viral entry makes it a target for therapies aimed at preventing herpes virus transmission. The protein's association with gD gH and gL is significant in the context of developing antiviral drugs and vaccines designed to disrupt the fusion process and reduce the severity of herpes-related symptoms. Understanding gB's function provides insights into potential therapeutic strategies against herpes simplex virus infections.

Product protocols

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

Target data

Envelope glycoprotein that forms spikes at the surface of virion envelope and binds to the host cell entry receptors MYH9/NMMHC-IIA and MYH10/NMMHC-IIB, promoting the virus entry into host cells. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell : following initial binding to its host cell entry receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation).
See full target information gB

Additional targets

gB,gB

Publications (44)

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

Journal of extracellular vesicles 14:e70152 PubMed40825575

2025

Extracellular Vesicles Containing MDP Derived from Lactobacillus rhamnosus GG Inhibit HSV-2 Infection by Activating the NOD2-IFN-I Signalling Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Jingyu Wang,Haoming Chen,Mei Huang,Yuqi Du,Ruyi Zhang,Yiyi Huang,Yuling Lin,Ruoru Pan,Yubing Wang,Wanqin Cui,Qian Wang,Lei Zheng,Xiumei Hu

BMC complementary medicine and therapies 25:245 PubMed40634910

2025

Insights into the antiviral mechanisms of β-caryophyllene: inhibiting viral spread and its synergy with acyclovir.

Applications

Unspecified application

Species

Unspecified reactive species

Mohammad Yasaghi,Sahar Beryani Dolatabadi,Ahad Yamchi,Alijan Tabarraei,Abdolvahab Moradi,Seyedeh Delafruz Hosseini

Iranian journal of microbiology 17:503-510 PubMed40612731

2025

Optimized isolation and purification of native glycoprotein B from herpes simplex virus 1: a streamlined approach.

Applications

Unspecified application

Species

Unspecified reactive species

Mohammad Yasaghi,Ahad Yamchi,Alijan Tabarraei,Sara Salari,Abdolvahab Moradi,Seyedeh Delafruz Hosseini

Clinical and translational medicine 15:e70353 PubMed40490945

2025

MLKL‒OPTN axis regulates herpesvirus-induced neurological sequelae.

Applications

Unspecified application

Species

Unspecified reactive species

Ilina Bhattacharya,Rashmi Kadam,Tejabhiram Yadavalli,Chandrashekhar D Patil,Hemant Borase,Ipsita Volety,Sergey Kalinin,Douglas L Feinstein,Henry C Tseng,Deepak Shukla

Brain : a journal of neurology 147:2552-2565 PubMed38366606

2024

HSV-1 reactivation results in post-herpetic neuralgia by upregulating Prmt6 and inhibiting cGAS-STING.

Applications

Unspecified application

Species

Unspecified reactive species

Erliang Kong,Tong Hua,Jian Li,Yongchang Li,Mei Yang,Ruifeng Ding,Haowei Wang,Huawei Wei,Xudong Feng,Chaofeng Han,Hongbin Yuan

Probiotics and antimicrobial proteins : PubMed37624569

2023

Lactobacillus rhamnosus GG Regulates Host IFN-I Through the RIG-I Signalling Pathway to Inhibit Herpes Simplex Virus Type 2 Infection.

Applications

Unspecified application

Species

Unspecified reactive species

Jingyu Wang,Mei Huang,Yuqi Du,Haoming Chen,Zixiong Li,Taiyu Zhai,Zihao Ou,Yiyi Huang,Fan Bu,Haojun Zhen,Ruoru Pan,Yubing Wang,Xiaohan Zhao,Bo Situ,Lei Zheng,Xiumei Hu

Microbiology spectrum 11:e0142123 PubMed37466427

2023

Several Alphaherpesviruses Interact Similarly with the NF-κB Pathway and Suppress NF-κB-Dependent Gene Expression.

Applications

Unspecified application

Species

Unspecified reactive species

Nicolás Romero,Alexander Tishchenko,Ruth Verhamme,Shelly M Wuerzberger-Davis,Cliff Van Waesberghe,Hans J Nauwynck,Shigeki Miyamoto,Herman W Favoreel

Acta pharmacologica Sinica 44:1856-1866 PubMed37193755

2023

Reducing lipid peroxidation attenuates stress-induced susceptibility to herpes simplex virus type 1.

Applications

Unspecified application

Species

Unspecified reactive species

Jing-Yu Weng,Xin-Xing Chen,Xiao-Hua Wang,Hui-Er Ye,Yan-Ping Wu,Wan-Yang Sun,Lei Liang,Wen-Jun Duan,Hiroshi Kurihara,Feng Huang,Xin-Xin Sun,Shu-Hua Ou-Yang,Rong-Rong He,Yi-Fang Li

Virology journal 20:8 PubMed36647143

2023

Ethanol extract from Artemisia argyi leaves inhibits HSV-1 infection by destroying the viral envelope.

Applications

Unspecified application

Species

Unspecified reactive species

Ping Liu,Lishan Zhong,Ji Xiao,Yuze Hu,Tao Liu,Zhe Ren,Yifei Wang,Kai Zheng

International journal of molecular sciences 23: PubMed36499174

2022

Complete and Prolonged Inhibition of Herpes Simplex Virus Type 1 Infection In Vitro by CRISPR/Cas9 and CRISPR/CasX Systems.

Applications

Unspecified application

Species

Unspecified reactive species

Dmitry S Karpov,Natalia A Demidova,Kirill A Kulagin,Anastasija I Shuvalova,Maxim A Kovalev,Ruslan A Simonov,Vadim L Karpov,Anastasiya V Snezhkina,Anna V Kudryavtseva,Regina R Klimova,Alla A Kushch
View all publications

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