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AB224744

Anti-Reston virus Nucleoprotein antibody

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(1 Publication)

Rabbit Polyclonal NCAP antibody. Suitable for WB and reacts with Recombinant fragment - Reston ebolavirus samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Reston ebolavirus - Reston NP aa 400 to C-terminus.

View Alternative Names

Nucleoprotein, Nucleocapsid protein, Reston NP, Protein N, rNP, NP

1 Images
Western blot - Anti-Reston virus Nucleoprotein antibody (AB224744)
  • WB

Supplier Data

Western blot - Anti-Reston virus Nucleoprotein antibody (AB224744)

This antibody has only been tested in WB using the recombinant protein, we have no data for endogenous protein.

All lanes:

Western blot - Anti-Reston virus Nucleoprotein antibody (ab224744) at 1/500 dilution

Lane 1:

80 ng recombinant protein

Lane 2:

60 ng recombinant protein

Lane 3:

40 ng recombinant protein

Secondary

All lanes:

Goat polyclonal to rabbit IgG at 1/50000 dilution

true

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Reston ebolavirus - Reston NP aa 400 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q91DE1

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"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Recombinant fragment - Reston ebolavirus": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/5000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
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.

Reston virus Nucleoprotein also known as Reston NP plays an essential role in the viral life cycle. It has a mass of approximately 75 kDa. This protein is found in cells infected by the Reston virus a member of the Filoviridae family which is part of the Ebola virus species. The nucleoprotein binds to the viral RNA genome forming a ribonucleoprotein complex that is involved in viral replication and packaging. This interaction is key for the virus to efficiently replicate and produce more viral particles inside the host cell.
Biological function summary

The Reston virus Nucleoprotein is involved in packaging the viral genome and interacts with other viral proteins to facilitate replication processes. The nucleoprotein associates with the viral polymerase complex which is needed for the synthesis of viral RNA. These associations are important for maintaining the structural stability of the viral capsid. Furthermore NP modulates the host immune response often by interfering with host antiviral defenses which helps the virus persist longer in host cells.

Pathways

The Reston virus Nucleoprotein operates within the viral replication and transcription pathways. The NP is involved in the encapsidation of the viral genome which is an important step in the formation of functional virions. It interacts with the viral polymerase L protein playing an important role in the transcription of viral messenger RNA. Such interactions are vital for initiating the transcription and replication mechanisms of the virus ensuring the viral genome's replication and spreading within an infected organism.

The Reston virus Nucleoprotein is often associated with Reston virus hemorrhagic fever although this virus subtype shows low pathogenicity in humans compared to other Ebola strains. Nevertheless understanding its role is important to prevent potential cross-species transmission that may increase pathogenicity. The nucleoprotein also shares similarities with the nucleoproteins of other Ebola virus strains which are more pathogenic in humans. These connections underline the importance of NP in studies of viral pathogenicity and immune evasion aiding in the development of potential therapeutic and preventive strategies.

Product protocols

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

Target data

Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Also recruits host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1.
See full target information NP

Publications (1)

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

Cancer management and research 12:7739-7751 PubMed32943922

2020

Exosomal Circ-ZNF652 Promotes Cell Proliferation, Migration, Invasion and Glycolysis in Hepatocellular Carcinoma via miR-29a-3p/GUCD1 Axis.

Applications

Unspecified application

Species

Unspecified reactive species

Yuhui Li,Hongliang Zang,Xue Zhang,Guomin Huang
View all publications

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