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AB74556

Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein

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(1 Publication)

Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein is a Dobrava-Belgrade orthohantavirus Full Length protein, expressed in Saccharomyces cerevisiae , with >95%, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

Nucleoprotein, Nucleocapsid protein, Protein N

1 Images
SDS-PAGE - Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein (AB74556)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Hantavirus Dobrava, strain Slovenia, nucleocapsid protein (AB74556)

SDS-PAGE showing ab74556 at approximately 50kDa. (2 μg/lane).

Key facts

Purity

>95% SDS-PAGE

Expression system

Saccharomyces cerevisiae

Tags

Tag free

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

Q805Q9

Animal free

No

Carrier free

No

Species

Dobrava-Belgrade orthohantavirus

Reconstitution

Reconstitute at 0.5 mg/mL in PBS

Storage buffer

Constituents: PBS

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"2 µg/mL", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"2 µg/mL", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1-2 µg/mL", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q805Q9","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
False

Supplementary information

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

The Hantavirus Dobrava strain Slovenia nucleocapsid protein also called N protein plays an important role in viral replication and assembly. This protein has a mass of approximately 50 kDa and is integral for encapsidating the viral RNA genome. It mainly expresses in infected host cells forming the basis of the ribonucleoprotein complex that is fundamental for the virus life cycle. The nucleocapsid protein serves as a scaffold for the construction of the viral capsid facilitating interactions with host cells' machinery.
Biological function summary

This nucleocapsid protein is involved in several critical processes for the virus. It forms part of a larger complex the ribonucleoprotein complex which includes the viral RNA and other key proteins. This complex serves as the template for replication and transcription of the viral genome ensuring the production of new viral particles. The N protein's ability to bind RNA and other nucleocapsid proteins makes it central to the regulation of these processes. Understanding its role provides insights into how hantaviruses hijack host cells for replication.

Pathways

The nucleocapsid protein from the Dobrava hantavirus strain participates in significant pathways related to viral replication and innate immune response evasion. It interacts with pathways involving the RIG-I-like receptor signaling helping the virus avoid detection by the host's immune system. Proteins such as RIG-I and MDA5 play a role here as they typically detect viral RNA but are often inhibited by this viral protein's functions allowing the virus to replicate undetected initially.

The nucleocapsid protein of the Dobrava hantavirus strain contributes to hemorrhagic fever with renal syndrome (HFRS) a severe disease caused by hantavirus infections. Its interaction with proteins such as interferon regulatory factors (IRFs) demonstrates its role in modulating immune responses exacerbating disease progression. Understanding the nucleocapsid's interactions and functions helps in identifying therapeutic targets to mitigate the effects of hantavirus-related diseases.

Specifications

Form

Lyophilized

Additional notes

Purified by chromatography under denaturing conditions.

General info

Function

Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity).

Sequence similarities

Belongs to the hantavirus nucleocapsid protein family.

Product protocols

Target data

Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity).
See full target information N

Publications (1)

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

Scientific reports 9:834 PubMed30696898

2019

Orthohantaviruses belonging to three phylogroups all inhibit apoptosis in infected target cells.

Applications

Unspecified application

Species

Unspecified reactive species

Carles Solà-Riera,Shawon Gupta,Hans-Gustaf Ljunggren,Jonas Klingström
View all publications

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