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AB256432

Crimean Congo Hemorrhagic Fever Virus Glycoprotein N (His tag)

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Crimean Congo Hemorrhagic Fever Virus Glycoprotein N (His tag) is a Crimean-Congo hemorrhagic fever virus strain IbAr10200 Fragment protein, in the 520 to 690 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.

View Alternative Names

Envelopment polyprotein, M polyprotein, GP

1 Images
SDS-PAGE - Crimean Congo Hemorrhagic Fever Virus Glycoprotein N (His tag) (AB256432)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Crimean Congo Hemorrhagic Fever Virus Glycoprotein N (His tag) (AB256432)

SDS-PAGE analysis of ab256432 under reducing conditions.

Key facts

Purity

>95% SDS-PAGE

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q8JSZ3

Animal free

No

Carrier free

No

Species

Crimean-Congo hemorrhagic fever virus strain IbAr10200

Storage buffer

pH: 7 - 8 Constituents: 0.64% Sodium chloride, 0.32% Tris HCl

storage-buffer

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Reactivity data

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

Avoid excessive mixing or shocking to prevent aggregation. Long-term storage above -80°C may result in aggregation and/or degradation.

Transmembrane region has been deleted and replaced with a His tag.

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Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":690,"aminoAcidStart":520,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q8JSZ3","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

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

Glycoprotein N also known as GP-N is a membrane-associated protein that plays an important role in viral assembly and replication. It has a molecular weight of approximately 40 kDa and is expressed on the surface of virions. Glycoprotein N forms a critical part of the virion envelope contributing to the stability and integrity of the viral particle. Researchers often examine its interactions with other viral and host proteins to understand its role more comprehensively.
Biological function summary

Glycoprotein N contributes to the recognition and fusion with host cell membranes. It is part of a larger viral envelope complex that directly involves glycoproteins and other structural proteins working together to facilitate viral entry into host cells. This protein's activity is important for the viral life cycle and infection processes. The effectiveness of viral propagation significantly depends on the functionality of this glycoprotein revealing its essential contribution to viral pathogenesis.

Pathways

Glycoprotein N significantly connects to the viral replication and assembly pathways. Within these pathways it frequently interacts with associated proteins such as Glycoprotein K and envelope glycoproteins. These interactions allow the viral proteins to coordinate effectively during the assembly of new virions ensuring a successful replication cycle. Understanding these interactions provides insights into how viral infections progress and helps identify potential therapeutic targets.

Glycoprotein N has a relevant connection to Crimean-Congo hemorrhagic fever. This severe viral disease links closely to the glycoprotein's role in viral entry and spread. The interactions of Glycoprotein N with the host's immune response proteins impact disease severity and progression. Additionally studies suggest its potential role in developing vaccine targets or antiviral therapies to manage and control this hemorrhagic fever and related viral diseases.
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Specifications

Form

Liquid

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General info

Function

Glycoprotein N. Plays a role in virion attachment to host receptor (PubMed : 38182887). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed : 19088291) Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (PubMed : 34793197).. Glycoprotein C. Binds to host cell surface receptor LDLR and mediates fusion between viral and cellular membranes (PubMed : 38182887). Attachment to receptor induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed : 19088291). Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (PubMed : 34793197, PubMed : 35234630). Exposure of the glycoprotein spikes to potassium is necessary for the conformational change leading to fusion (By similarity).

Sequence similarities

Belongs to the nairovirus envelope glycoprotein family.

Post-translational modifications

Envelopment polyprotein. Specific enzymatic cleavage by host MBTPS1/S1P/SKI-1 endopeptidase yield glycoprotein N (PubMed:12885882, PubMed:17898072, PubMed:25933376). Specific enzymatic cleavages by host furin-like protease and MBTPS1/S1P endopeptidase yield GP38 (PubMed:25933376).. Glycoprotein N. Glycosylated.. Glycoprotein C. Glycosylated.

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Product protocols

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Target data

Glycoprotein N. Plays a role in virion attachment to host receptor (PubMed : 38182887). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed : 19088291) Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (PubMed : 34793197).. Glycoprotein C. Binds to host cell surface receptor LDLR and mediates fusion between viral and cellular membranes (PubMed : 38182887). Attachment to receptor induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed : 19088291). Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (PubMed : 34793197, PubMed : 35234630). Exposure of the glycoprotein spikes to potassium is necessary for the conformational change leading to fusion (By similarity).
See full target information GP
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