Recombinant Zaire ebolavirus Nucleoprotein (NP), partial, Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus), Yeast, N-terminal 6xHis-tagged, 31.1kDa, purity >90% as determined by SDS-PAGE.
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Recombinant Zaire ebolavirus Nucleoprotein (NP), partial

Recombinant Zaire ebolavirus Nucleoprotein (NP), partial — Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. Purity >90%.

SKU: BCRECP-003897 Categories: , ,
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Product Specifications

Product SkuBCRECP-003897
Product DescriptionRecombinant Zaire ebolavirus Nucleoprotein (NP) Protein is expressed from Yeast with N-terminal 6xHis-tagged. It contains 488-739aa. [Accession | P18272].
Uniprot No.P18272
Gene NamesNP
PurityGreater than 90% as determined by SDS-PAGE.
Expression SystemYeast
Expression Region488-739aa
SpeciesZaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Tag InfoN-terminal 6xHis-tagged
Molecular weight31.1kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasOthers

Function

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.

Biological Context

Subcellular Location: Virion; Host cytoplasm

Product Specifications

Recombinant Zaire ebolavirus Nucleoprotein (NP), partial is a recombinant protein from Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus), expressed in Yeast, covering amino acids 488-739aa, with N-terminal 6xHis-tagged tag, molecular weight 31.1kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

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Protein Biology

Function

Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:16719918, PubMed:25865894, PubMed:26119732, PubMed:30333622). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:25865894, PubMed:26119732). Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released (PubMed:29144446). 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 (PubMed:22247782). Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid (PubMed:30333622). Also recruits host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription (PubMed:27755595, PubMed:29290611). Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1 (PubMed:28794491, PubMed:30301857)

Subcellular Location

Virion; Host cytoplasm

Subunit

Homooligomer. Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. Interacts with VP35 and VP30 to form the nucleocapsid (PubMed:12191476, PubMed:25865894, PubMed:25910597, PubMed:26119732, PubMed:27755595). Interacts with host PPP2R5C; this interaction leads to VP30 dephosphorylation and viral transcription (PubMed:29290611). Interacts with VP24; this interaction facilitates nucleocapsid assembly and genome packaging (PubMed:12191476, PubMed:28794491, PubMed:29144446, PubMed:29339477). Interacts with matrix protein VP40; this interaction allows recruitment of the nucleocapsid into progeny virions (PubMed:17229682). Interacts with host STAU1 (PubMed:30301857). Interacts with host NXF1 (via RNA-binding domain); this interaction recruits NXF1 to the inclusion bodies were viral replication takes place, probably to export viral mRNA-NXF1 complexes from these sites (PubMed:31940815). Interacts with host CCDC92; this interaction sequesters NP in the host cytoplasm (PubMed:32528005). Interacts with host TRIM14 (PubMed:37562033)

Gene: NP  |  Organism: Zaire ebolavirus (strain Mayinga-76)  |  Synonyms: Ebola NP; Nucleocapsid protein
Key Publications

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How do I order or inquire about this product?

Submit the Online Inquiry form with your required quantity and specifications, or email sales@biocrestsci.com. Available sizes, pricing, stock status, documentation, and estimated lead time are confirmed in the formal quotation.

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Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

How should this product be stored?

Follow the storage and handling instructions in the product-specific datasheet and Certificate of Analysis (CoA). Requirements may vary by product form and formulation; contact BioCrest Sci if product-specific guidance is needed.

What quality controls are performed on your products?

Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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