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:
在線留言
中文名稱:
Recombinant Human SARS coronavirus Nucleoprotein(N)
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.
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. May modulate transforming growth factor-beta signaling by binding host SMAD3.
基因功能參考文獻:
The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. PMID: 28148787
Electrostatic repulsion acts as a switch to regulate SARS virus N protein oligomerization. PMID: 23717688
These results suggest that SARS coronavirus could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease. PMID: 22222284
The co-localization of SARS-CoVN and CXCL16 in the cytoplasm of HEK293FT cells was also shown using confocal laser scanning microscopy. PMID: 20960183
The HLA-A 2402 complexed with SARSV N1 showed a novel host strategy to present an immunodominant CTL epitope by intrachain hydrogen bond as a featured epitope. PMID: 20844028
SARS-CoV N interacts with MAP19 and increased the expression of MAP19 in cells. PMID: 19737459
This is the first report showing the ability of the nucleocapsid protein of SARS-CoV to induce apoptosis and actin reorganization in mammalian cells under stressed conditions. PMID: 15294014
analysis of SARS-CoV nucleocapsid protein expressed in insect cells PMID: 15514849
The nucleocapsid protein of the SARS coronavirus was cloned and purified. PMID: 15523835
Binding to cyclophilin A during invasion of host cells. PMID: 15688292
coronavirus N protein undergoes posttranslational modification by sumoylation; functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions PMID: 15848177
the nucleocapsid protein forms a dimer through its C-terminal domain PMID: 15849181
Differences in nuclear/nucleolar localization properties of N from other members of coronavirus family suggest a unique shuttle protein function for N, which may play an important role in the pathogenesis of SARS. PMID: 15992957
results showed that the SARS-CoV N protein can significantly activate NF-kappaB only in Vero E6 cells, which are susceptible to SARS-CoV infection, but not in Vero or HeLa cells; suggests that NF-kappaB activation is cell-specific PMID: 16143815
The secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. PMID: 16214138
Results show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. PMID: 16228284
data suggest that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation PMID: 16285739
cytoplasmic localization was directed by region III and was the dominant localization signal in the N protein. PMID: 16298975
the S phase inhibitory activity of the N protein may have major significance during viral pathogenesis PMID: 16431923
the N protein has a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo PMID: 16627473
using the solution structure of severe acute respiratory (SARS) coronavirus N-protein, revealed that this motif is available for interaction with cellular factors which may mediate nucleolar localization PMID: 16734668
This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV. PMID: 16998888
the nucleocapsid protein of severe acute respiratory syndrome coronavirus is sumoylated by interaction with Ubc9 PMID: 17037517
characterization of the structures of N protein N-terminal domain in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively PMID: 17229691
The C-terminal domain (CTD), spanning residues 248-365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. The crystal structure of the NP248-365 region is solved, suggesting a mechanism for helical RNA packaging in the virus. PMID: 17379242
SARS coronavirus N protein can induce apoptosis of COS-1 cells by activating mitochondrial pathway PMID: 17453707
We also showed that N protein activated IL-6 expression through NF-kappaB by facilitating the translocation of NF-kappaB from cytosol to nucleus. PMID: 17490702
SARS coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling PMID: 18055455
The experiments revealed that N induces the intrinsic apoptotic pathway, resulting in processing of N at residues 400 and 403 by caspase-6 and/or caspase-3. PMID: 18155731
fgl2 gene transcription induced by the N protein of SARS-CoV was dependent on transcription factor C/EBP alpha binding with its cognate cis-element in fgl2 promoter. PMID: 18390877
It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1, inhibiting protein translation and cytokinesis by blocking F-actin bundling. PMID: 18448518
This study employed the SAIL method to determine the high-quality solution structure of the severe acute respiratory syndrome coronavirus nucleocapsid protein C-terminal domain by NMR. PMID: 18561946
the domain conferring the ability to direct virus-like particle assembly and release in SARS-CoV N is largely contained between residues 168 and 421 PMID: 18592403
Phosphorylation of the arginine/serine motif of the nucleocapsid protein did not significantly affect RNA binding of the nucleocapsid protein but impaired its multimerization ability. PMID: 18631359
This paper describes the work to identify two proteins/protein fragments of N protein and to determine their source. PMID: 18926799
An excessive host immune response against the nucleocapsid protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is involved in severe pneumonia caused by SARS-CoV infection. PMID: 18941225
The SARS-CoV N protein is a modular protein containing multiple RNA-binding sites. PMID: 19052082
thermostability of the N-terminal RNA-binding domain (RBD) of the N protein; results showed the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90% PMID: 19254548
SR-rich motif is critical for effective virus replication. PMID: 19370068
SARS-CoV N protein specifically modulates transcription of the FGL2 gene to cause fibrosis and vascular thrombosis. PMID: 19423547