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, with >95% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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).
Envelopment polyprotein, M polyprotein, GP
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, with >95% purity and suitable for SDS-PAGE.
pH: 7 - 8
Constituents: 0.64% Sodium chloride, 0.32% Tris HCl
Glycoprotein N
Belongs to the nairovirus envelope glycoprotein family.
Envelopment polyprotein
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.
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.
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.
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.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
SDS-PAGE analysis of ab256432 under reducing conditions.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com