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AB53479

Anti-HSV2 gC antibody [H1196]

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(1 Publication)

Mouse Monoclonal GC antibody. Carrier free. Suitable for ICC/IF and reacts with Human herpesvirus 2 samples. Cited in 1 publication.

View Alternative Names

Glycoprotein C, Herpes Simplex Virus 2 glycoprotein C, Human Herpsevirus 2, UL44

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

H1196

Isotype

IgG

Carrier free

Yes

Reacts with

Human herpesvirus 2

Applications

ICC/IF

applications

Specificity

Reactive with gC-2 of Herpes Simplex Virus 2.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human herpesvirus 2": { "WB-species-checked": "notRecommended", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>", "ICCIF-species-checked": "guaranteed", "ICCIF-species-dilution-info": "10 µg/mL", "ICCIF-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
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.

HSV2 gC also known as Herpes Simplex Virus Type 2 glycoprotein C functions mechanically as an essential viral protein for the virus's adherence to host cells. This glycoprotein with a mass of approximately 50 kDa facilitates the initial attachment phase by binding to glycosaminoglycans on the surface of epithelial and neuronal cells. Expressed on the virion envelope and cell membrane HSV2 gC plays a critical role in the infection process by enabling stable contact between the virus and host cell surfaces. This initiates subsequent steps essential for viral entry and replication.
Biological function summary

HSV2 gC contributes significantly to HSV-2’s pathogenic profile. It is a part of the complex viral machinery that masks the virus from the host immune system. By binding to complement component C3b it impairs the complement cascade reducing opsonization and phagocytosis. This evasion of immune responses permits the virus to efficiently establish infection and persistence within the host. Furthermore the interaction of gC with host cells amplifies virus attachment efficiency facilitating viral transmission and spread.

Pathways

HSV2 gC affects host-pathogen dynamics in pathways related to immune suppression and infection propagation. The interaction with complement pathways demonstrates its role in inhibiting the activation of these critical immune pathways allowing the virus to evade early host immune detection. A related protein in these pathways is glycoprotein B (gB) which assists in fusion. Together these glycoproteins form a concerted mechanism that ensures effective viral entry and evasion of host defenses highlighting the importance of HSV2 gC in maintaining viral survival.

HSV2 gC is directly associated with genital herpes an infection significantly affecting the global population. This glycoprotein not only contributes to initial infection but also plays a role in the recurrence of lesions by enabling the virus to evade immune detection. HSV2 gC links to glycoprotein D (gD) another critical viral glycoprotein involved in cell entry emphasizing the collaborative nature of these proteins in disease manifestation. The understanding of HSV2 gC's role enhances strategies for targeted therapies and vaccine developments aimed at reducing transmission and symptomatic episodes.

Product protocols

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

Publications (1)

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

Autophagy 13:1064-1075 PubMed28453381

2017

Degradation of protein translation machinery by amino acid starvation-induced macroautophagy.

Applications

Unspecified application

Species

Unspecified reactive species

Christine Gretzmeier,Sven Eiselein,Gregory R Johnson,Rudolf Engelke,Heike Nowag,Mostafa Zarei,Victoria Küttner,Andrea C Becker,Kristoffer T G Rigbolt,Maria Høyer-Hansen,Jens S Andersen,Christian Münz,Robert F Murphy,Jörn Dengjel
View all publications

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