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AB43048

Recombinant HSV1 gG Envelope Protein

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(1 Publication)

Recombinant HSV1 gG Envelope Protein is a Human alphaherpesvirus 1 strain 17 Fragment protein, expressed in Escherichia coli, with >95%, suitable for ELISA, WB.

View Alternative Names

US4, gG, Envelope glycoprotein G, gG-1

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

WB, ELISA

applications

Biologically active

No

Accession

P06484

Animal free

No

Carrier free

No

Species

Human alphaherpesvirus 1 strain 17

Storage buffer

Constituents: 50% Glycerol (glycerin, glycerine), 0.395% Tris HCl, 0.0292% EDTA

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P06484","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

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

The HSV1 gG envelope protein also known as glycoprotein G is an important part of the Herpes Simplex Virus 1. This protein has a molecular mass of approximately 71 kDa. It is a type I membrane protein found in the viral envelope and on the surface of infected host cells. Glycoprotein G plays a role in viral attachment and entry into the host cells helping the virus infect and propagate within the host organism.
Biological function summary

Glycoprotein G assists in the immune evasion by binding to host immune modulators reducing immune detection. Glycoprotein G is part of the larger complex involved in viral infection along with other glycoproteins such as gB gD and gH. These components work together to facilitate the fusion of the viral and host cell membranes which allows viral entry into the host cell.

Pathways

Glycoprotein G participates in the viral entry pathway and immune modulation pathways. In the viral entry pathway it interacts with other viral glycoproteins like gD which binds to host cell receptors like nectin-1. This interaction is important for the viral fusion process. The immune modulation pathway involves interference with host immune responses where glycoprotein G assists in decreasing the recognition by host antibodies.

Glycoprotein G expression relates to Herpes Simplex Virus type 1 (HSV-1) infections and complications such as herpes labialis and encephalitis. These infections can result in recurrent lesions around the oral or facial area and severe complications in neural tissues. Glycoprotein G has connections to other viral proteins like glycoprotein B and D through its role in initiating viral infections contributing to disease progression and symptom manifestations.

Specifications

Form

Liquid

Additional notes

Sepharose derived purification.

General info

Function

Chemokine-binding protein that inhibits neutrophils' chemotaxis.

Sequence similarities

Belongs to the alphaherpesvirinae glycoprotein G family.

Product protocols

Target data

Chemokine-binding protein that inhibits neutrophils' chemotaxis.
See full target information gG

Additional targets

HSV1 gG Envelope Protein

Publications (1)

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

The Journal of clinical investigation 131: PubMed34618692

2021

Trivalent nucleoside-modified mRNA vaccine yields durable memory B cell protection against genital herpes in preclinical models.

Applications

Unspecified application

Species

Unspecified reactive species

Sita Awasthi,James J Knox,Angela Desmond,Mohamad-Gabriel Alameh,Brian T Gaudette,John M Lubinski,Alexis Naughton,Lauren M Hook,Kevin P Egan,Ying K Tam,Norbert Pardi,David Allman,Eline T Luning Prak,Michael P Cancro,Drew Weissman,Gary H Cohen,Harvey M Friedman
View all publications

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