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AB252726

Anti-Norovirus Major Capsid Protein antibody [B1938M]

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(1 Publication)

Mouse Monoclonal Norovirus Major Capsid Protein antibody. Carrier free. Suitable for ELISA and reacts with Norovirus samples. Cited in 1 publication. Immunogen corresponding to Virus preparation containing Norovirus Major Capsid Protein protein.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

B1938M

Isotype

IgG1

Carrier free

Yes

Reacts with

Norovirus

Applications

ELISA

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Specificity

Recognizes Norovirus virus-like particle (VLP) from GI and GII, specific for a conserved epitope of the major capsid protein.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ELISA" : {"fullname" : "ELISA", "shortname":"ELISA"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Norovirus": { "ELISA-species-checked": "guaranteed", "ELISA-species-dilution-info": "", "ELISA-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Purification notes
Purified from tissue culture supernatant. > 85% pure (size-exclusion chromatography).
Storage buffer
Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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.

The Norovirus Major Capsid Protein also known as VP1 plays a central role in the formation of the viral capsid a protective shell that encases the viral RNA. It has an approximate molecular mass of 58 kDa. This protein assembles into icosahedral structures that are critical for the virus structure and infectivity. Expression of VP1 occurs in infected host cells where newly synthesized viruses are produced.
Biological function summary

The major capsid protein of norovirus ensures the protection of viral genetic material and facilitates attachment to host cell receptors. Although VP1 is not part of a complex itself it oligomerizes to form the full capsid structure. By doing so VP1 allows the virus to survive in the host environment aiding in the viral entry into host cells and subsequent replication within them.

Pathways

The Norovirus Major Capsid Protein interacts with host cell receptor binding pathways which are essential for viral entry. It is closely associated with endocytic pathways that facilitate internalization into the cell. VP1's interaction with cellular receptors such as histo-blood group antigens plays a major role in these pathways highlighting its significance in viral infection processes.

Norovirus infections are a common cause of acute gastroenteritis worldwide. The capsid protein VP1 is critical in determining virulence and host specificity. It connects with other viral proteins in the replication complex influencing disease progression. Understanding the interactions and role of VP1 can aid in developing therapeutic strategies against norovirus-linked diarrheal diseases.

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

Current protocols 4:e1030 PubMed38923763

2024

Applications of Surface Plasmon Resonance (SPR) to the Study of Diverse Protein-Ligand Interactions.

Applications

Unspecified application

Species

Unspecified reactive species

Dana M Burris,Samuel W Gillespie,Emma Joy Campbell,S Nick Ice,Vikas Yadav,William D Picking,Christian L Lorson,Kamal Singh
View all publications

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