Recombinant Measles virus Nucleoprotein (N), partial

中文名稱：

Recombinant Measles virus Nucleoprotein(N) ,partial
貨號：

CSB-YP894340MCV
說明書：

MSDS Datasheet
規格：
來源：

Yeast
其他：

中文名稱：

Recombinant Measles virus Nucleoprotein(N) ,partial
貨號：

CSB-EP894340MCV
說明書：

MSDS Datasheet
規格：
來源：

E.coli
其他：

中文名稱：

Recombinant Measles virus Nucleoprotein(N) ,partial
貨號：

CSB-EP894340MCV-B
說明書：

MSDS Datasheet
規格：
來源：

E.coli
共軛：

Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
其他：

中文名稱：

Recombinant Measles virus Nucleoprotein(N) ,partial
貨號：

CSB-BP894340MCV
說明書：

MSDS Datasheet
規格：
來源：

Baculovirus
其他：

中文名稱：

Recombinant Measles virus Nucleoprotein(N) ,partial
貨號：

CSB-MP894340MCV
說明書：

MSDS Datasheet
規格：
來源：

Mammalian cell
其他：

產品詳情
產品評價
靶點詳情

產品詳情

純度：

>85% (SDS-PAGE)
基因名：

N
Uniprot No.：

Q9WMB5
別名：

N; NP; Nucleoprotein; Nucleocapsid protein; NP; Protein N
種屬：

Measles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose panencephalitis virus)
蛋白長度：

Partial
蛋白標簽：

Tag?type?will?be?determined?during?the?manufacturing?process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
產品提供形式：

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
復溶：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲存條件：

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

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期：

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet ：

Please contact us to get it.

產品評價

靶點詳情

功能：

Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases. N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response. Ntail binds to a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth arrest.
基因功能參考文獻：
1. Two mechanisms, namely, the system tending to adopt the structure in which the free energy of isolated alpha-helical molecular recognition element (alpha-MoRE-MeV) is the minimum, and the binding energy of alpha-MoRE-MeV to its partner protein XD tending to the minimum, jointly dominate the coupled folding and binding process. PMID: 27423742
2. The structure reveals the molecular details of the conserved N(0)-P interface and explains how P chaperones N(0), preventing both self-assembly of N(0) and its binding to RNA. PMID: 26719278
3. Report genetic characterization of N protein isolated from measles virus responsible for disease outbreaks in the Philippines. PMID: 26036942
4. A folding after binding mechanism has been demonstrated in the recognition between the measles virus NTAIL and X domains. PMID: 25511246
5. Loss of the P-N interaction results in reduced transcription. PMID: 25008930
6. TBK1 plays a critical role in mediating the effects of MVNP on osteoclast differentiation and on the expression of IL-6, a key contributor to the pagetic osteoclast phenotype. PMID: 23794264
7. Phosphorylation at T279 is a prerequisite for successful nucleocapsid formation. PMID: 24198432
8. These results suggest that nucleoprotein-phosphorylation is also involved in viral genomic RNA stability. PMID: 23966404
9. Data indicate two clusters represented by the 466 nucleoprotein (N) sequences. PMID: 23056226
10. The intrinsically disordered C-terminal domain (N(TAIL) )of measles virus (MeV) nucleoprotein undergoes alpha-helical folding upon binding to the C-terminal X domain (XD) of the phosphoprotein. This study re-evaluate the role of Box3 in N(TAIL)-XD binding. PMID: 22887965
11. Isolated strains were phylogenetically analysed according to the nucleotide sequence of the C-terminal region of the nucleoprotein gene amplified by RT-PCR. Six isolates identified were all clustered within genotype H1. PMID: 22117136
12. the N-tail regulatory domain acts by mediating the interaction with other factors that may positively or negatively influence RNA polymerase function. PMID: 22318731
13. Nucleocapsid protein of measles virus blocks host IFN-alpha/beta and gamma- responses. PMID: 22226324
14. Phosphorylation and acetylation post-translational modification sites located PMID: 20925409
15. Data show that hsp70 binding to the C-terminal domain N(TAIL)of the nucleocapsid protein requires an hsp40 co-chaperone that interacts primarily with the hsp70 nucleotide binding domain (NBD) and displays no significant affinity for N(TAIL). PMID: 19718689
16. A structural model of the complex between a domain of the measles virus nucleoprotein (nucleocapsid protein) and a domain of the measles virus phosphoprotein. PMID: 16046624
17. MV-N targets eIF3-p40 and may be involved in inhibiting MV-induced host translation PMID: 17686838
18. the phosphorylation of N protein is important in the activation of the transcription of viral mRNA and/or replication of the genome in vivo PMID: 18442172
19. The region of the intrinsically disordered C-terminal domain of measles virus nucleoprotein (N(TAIL)) that undergoes induced folding, was mapped. PMID: 18536007
20. Viral N protein consists of a structured core and an intrinsically disordered C-terminal domain. PMID: 19198564
21. The interaction between the measles virus nucleoprotein and IRF3 relies on human cellular co-factors. PMID: 19445677
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亞細胞定位：

Virion. Host cytoplasm.
蛋白家族：

Paramyxoviruses nucleocapsid family
數據庫鏈接：

KEGG: vg:1489804