GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Nucleoprotein (Nucleocapsid protein) (Protein N)

 NCAP_I34A1              Reviewed;         498 AA.
P03466; Q20N34; Q58NB3; Q67228; Q80AB4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
16-JAN-2019, entry version 114.
RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04070};
AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04070};
Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04070};
Name=NP {ECO:0000255|HAMAP-Rule:MF_04070};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7292985; DOI=10.1016/0042-6822(81)90223-3;
Winter G., Fields S.;
"The structure of the gene encoding the nucleoprotein of human
influenza virus A/PR/8/34.";
Virology 114:423-428(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6166474; DOI=10.1111/j.1432-1033.1981.tb05341.x;
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
"Complete nucleotide sequence of the nucleoprotein gene from the human
influenza strain A/PR/8/34 (HON1).";
Eur. J. Biochem. 116:347-353(1981).
[3]
ERRATUM, AND SEQUENCE REVISION.
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.;
Eur. J. Biochem. 116:645-645(1981).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16136460; DOI=10.1086/444546;
van Baalen C.A., Kwa D., Verschuren E.J., Reedijk M.L., Boon A.C.,
de Mutsert G., Rimmelzwaan G.F., Osterhaus A.D., Gruters R.A.;
"Fluorescent antigen-transfected target cell cytotoxic T lymphocyte
assay for ex vivo detection of antigen-specific cell-mediated
cytotoxicity.";
J. Infect. Dis. 192:1183-1190(2005).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[8]
SUBCELLULAR LOCATION.
PubMed=9770415; DOI=10.1006/viro.1998.9329;
Weber F., Kochs G., Gruber S., Haller O.;
"A classical bipartite nuclear localization signal on Thogoto and
influenza A virus nucleoproteins.";
Virology 250:9-18(1998).
[9]
SUBCELLULAR LOCATION.
PubMed=9971805;
Digard P., Elton D., Bishop K., Medcalf E., Weeds A., Pope B.;
"Modulation of nuclear localization of the influenza virus
nucleoprotein through interaction with actin filaments.";
J. Virol. 73:2222-2231(1999).
[10]
SUBUNIT, AND MUTAGENESIS OF ARG-199; ARG-416 AND PHE-479.
PubMed=10405371; DOI=10.1006/viro.1999.9818;
Elton D., Medcalf E., Bishop K., Digard P.;
"Oligomerization of the influenza virus nucleoprotein: identification
of positive and negative sequence elements.";
Virology 260:190-200(1999).
[11]
RNA-BINDING, AND MUTAGENESIS OF ARG-8; TRP-104; TRP-120; TRP-139;
TYR-148; ARG-150; ARG-156; ARG-175; ARG-199; ARG-204; TRP-207;
ARG-208; ARG-213; ARG-267; TRP-330; TRP-386; ARG-391; PHE-412 AND
ARG-416.
PubMed=10438825;
Elton D., Medcalf L., Bishop K., Harrison D., Digard P.;
"Identification of amino acid residues of influenza virus
nucleoprotein essential for RNA binding.";
J. Virol. 73:7357-7367(1999).
[12]
INTERACTION WITH HUMAN XPO1.
PubMed=11119609; DOI=10.1128/JVI.75.1.408-419.2001;
Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R.,
McCauley J., Digard P.;
"Interaction of the influenza virus nucleoprotein with the cellular
CRM1-mediated nuclear export pathway.";
J. Virol. 75:408-419(2001).
-!- FUNCTION: Encapsidates the negative strand viral RNA, protecting
it from nucleases. The encapsidated genomic RNA is termed the
ribonucleoprotein (RNP) and serves as template for transcription
and replication. The RNP needs to be localized in the host nucleus
to start an infectious cycle, but is too large to diffuse through
the nuclear pore complex. NP comprises at least 2 nuclear
localization signals that are responsible for the active RNP
import into the nucleus through cellular importin alpha/beta
pathway. Later in the infection, nclear export of RNPs are
mediated through viral proteins NEP interacting with M1 which
binds nucleoproteins. It is possible that nucleoprotein binds
directly host exportin-1/XPO1 and plays an active role in RNPs
nuclear export. M1 interaction with RNP seems to hide
nucleoprotein's nuclear localization signals. Soon after a virion
infects a new cell, M1 dissociates from the RNP under
acidification of the virion driven by M2 protein. Dissociation of
M1 from RNP unmasks nucleoprotein's nuclear localization signals,
targeting the RNP to the nucleus. {ECO:0000255|HAMAP-
Rule:MF_04070}.
-!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind host
exportin-1/XPO1. Binds to viral genomic RNA. Protein-RNA contacts
are mediated by a combination of electrostatic interactions
between positively charged residues and the phosphate backbone and
planar interactions between aromatic side chains and bases.
{ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:10405371}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2547640, EBI-2547640;
O43707:ACTN4 (xeno); NbExp=2; IntAct=EBI-2547640, EBI-351526;
O60684:KPNA6 (xeno); NbExp=5; IntAct=EBI-2547640, EBI-359923;
P03485:M; NbExp=2; IntAct=EBI-2547640, EBI-2547543;
P03433:PA; NbExp=3; IntAct=EBI-2547640, EBI-2547616;
P03431:PB1; NbExp=5; IntAct=EBI-2547640, EBI-2547514;
P03428:PB2; NbExp=3; IntAct=EBI-2547640, EBI-2547475;
Q8WV44:TRIM41 (xeno); NbExp=5; IntAct=EBI-2547640, EBI-725997;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04070,
ECO:0000269|PubMed:9770415, ECO:0000269|PubMed:9971805}.
-!- PTM: Late in virus-infected cells, may be cleaved from a 56-kDa
protein to a 53-kDa protein by a cellular caspase. This cleavage
might be a marker for the onset of apoptosis in infected cells or
have a specific function in virus host interaction.
{ECO:0000255|HAMAP-Rule:MF_04070}.
-!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family.
{ECO:0000255|HAMAP-Rule:MF_04070}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; V01084; CAA24268.1; -; Genomic_RNA.
EMBL; J02147; AAA43467.1; -; Genomic_RNA.
EMBL; AF389119; AAM75159.1; -; Genomic_RNA.
EMBL; EF467822; ABO21710.1; -; Genomic_RNA.
EMBL; AY936882; AAX39501.1; -; Genomic_RNA.
EMBL; CY009447; ABD77679.1; -; Genomic_RNA.
RefSeq; NP_040982.1; NC_002019.1.
PDB; 2BST; X-ray; 2.10 A; C=383-391.
PDB; 2WFS; EM; 12.00 A; A/B/C/D/E/F/G/H/I=8-498.
PDB; 4NQV; X-ray; 2.39 A; M/N/O/P/Q/R=44-52.
PDB; 4ZDU; X-ray; 2.30 A; B=2-15.
PDB; 5NPZ; X-ray; 1.43 A; C=252-260.
PDB; 5NQ3; X-ray; 1.57 A; C/F=252-260.
PDB; 5V5O; X-ray; 2.24 A; A/B=198-216.
PDBsum; 2BST; -.
PDBsum; 2WFS; -.
PDBsum; 4NQV; -.
PDBsum; 4ZDU; -.
PDBsum; 5NPZ; -.
PDBsum; 5NQ3; -.
PDBsum; 5V5O; -.
ProteinModelPortal; P03466; -.
SMR; P03466; -.
DIP; DIP-43998N; -.
IntAct; P03466; 149.
MINT; P03466; -.
PRIDE; P03466; -.
GeneID; 956531; -.
KEGG; vg:956531; -.
KO; K19391; -.
OrthoDB; 1638at10239; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-192814; vRNA Synthesis.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-192869; cRNA Synthesis.
Reactome; R-HSA-192905; vRNP Assembly.
EvolutionaryTrace; P03466; -.
PRO; PR:P03466; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; TAS:Reactome.
GO; GO:0019070; P:viral genome maturation; TAS:Reactome.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
HAMAP; MF_04070; INFV_NCAP; 1.
InterPro; IPR002141; Flu_NP.
Pfam; PF00506; Flu_NP; 1.
1: Evidence at protein level;
3D-structure; Capsid protein; Complete proteome;
Helical capsid protein; Host nucleus; Host-virus interaction;
Reference proteome; Ribonucleoprotein; RNA-binding;
Viral nucleoprotein; Viral penetration into host nucleus; Virion;
Virus entry into host cell.
CHAIN 1 498 Nucleoprotein.
/FTId=PRO_0000079092.
MOTIF 1 18 Unconventional nuclear localization
signal. {ECO:0000255|HAMAP-
Rule:MF_04070}.
MOTIF 198 216 Bipartite nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04070}.
MUTAGEN 8 8 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 104 104 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 120 120 W->A: Partial loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 139 139 W->A: Partial loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 148 148 Y->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 150 150 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 156 156 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 175 175 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 199 199 R->A: 60% loss of Homomultimerization
affinity. No effect on RNA-binding
activity. {ECO:0000269|PubMed:10405371,
ECO:0000269|PubMed:10438825}.
MUTAGEN 204 204 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 207 207 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 208 208 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 213 213 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 267 267 R->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 330 330 W->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 386 386 W->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 391 391 R->A: No effect on RNA-binding activity.
{ECO:0000269|PubMed:10438825}.
MUTAGEN 412 412 F->A: Complete loss of RNA-binding
activity. {ECO:0000269|PubMed:10438825}.
MUTAGEN 416 416 R->A: Complete loss of
Homomultimerization. Complete loss of
RNA-binding activity.
{ECO:0000269|PubMed:10405371,
ECO:0000269|PubMed:10438825}.
MUTAGEN 479 479 F->A: 2-fold increase of self
association.
{ECO:0000269|PubMed:10405371}.
CONFLICT 135 135 H -> N (in Ref. 1; CAA24268).
CONFLICT 247 247 N -> D (in Ref. 1; CAA24268).
CONFLICT 353 353 L -> V (in Ref. 1; CAA24268).
CONFLICT 425 425 I -> V (in Ref. 1; CAA24268).
CONFLICT 430 430 N -> T (in Ref. 1; CAA24268).
HELIX 10 13 {ECO:0000244|PDB:4ZDU}.
SEQUENCE 498 AA; 56210 MW; 4F750FEF05D6E668 CRC64;
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS DYEGRLIQNS
LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV NGKWMRELIL YDKEEIRRIW
RQANNGDDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
AAVKGVGTMV MELVRMIKRG INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD
QVRESRNPGN AEFEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT KVLPRGKLST
RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISIQP TFSVQRNLPF
DRTTIMAAFN GNTEGRTSDM RTEIIRMMES ARPEDVSFQG RGVFELSDEK AASPIVPSFD
MSNEGSYFFG DNAEEYDN


Related products :

Catalog number Product name Quantity
SCH-OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
SCH-OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
SCH-OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
SCH-OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
orb81559 Hepatitis Virus Nucleocapsid (core) Genotype-3a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81557 Hepatitis Virus Nucleocapsid (core) Genotype-2a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81561 Hepatitis Virus Nucleocapsid (core) Genotype-4 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81567 Hepatitis Virus Nucleocapsid (core) (105-302) protein The E.coli derived recombinant protein from E1 region contains the HCV core nucleocapsid immunodominant regions, amino acids 105-302. The protein 100
orb81769 Measles Virus Nucleocapsid protein The E.coli derived recombinant protein contains the nucleocapsid immunodominant regions, 89-165 amino acids. For research use only. 100
orb81568 Hepatitis Virus Nucleocapsid (core) 24 protein The HCV Core 24 genotype-1b, E.coli derived recombinant protein, contains the HCV core nucleocapsid immunodominant regions. The protein is fused with b-g 100
orb81570 Hepatitis Virus Nucleocapsid (core) 22kDa protein The E.coli derived recombinant protein contains the HCV core nucleocapsid genotype 1b, immunodominant regions, amino acids 2-192, 22kDa.The protein is 100
orb81638 Hantavirus protein The Hantavirus nucleocapsid (N) fusion protein protein is expressed in E.coli and fused to GST-tag having Mw of 37 kDa. Hantavirus nucleocapsid (N) is conserved among different stra 100
orb81555 Hepatitis Virus Nucleocapsid (core) Genotype-1a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. For research use only. 100
orb81563 Hepatitis Virus Nucleocapsid (core) Genotype-6a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. For research use only. 100
orb81554 Hepatitis Virus Nucleocapsid (core) Genotype-1 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 1-102. For research use only. 100
orb81560 Hepatitis Virus Nucleocapsid (core) Genotype-3b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. For research use only. 100
orb81562 Hepatitis Virus Nucleocapsid (core) Genotype-5 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. For research use only. 100
orb81564 Hepatitis Virus Nucleocapsid (core) Genotype-3_10 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. For research use only. 100
orb81572 Hepatitis Virus Nucleocapsid (core) 22kDa, Fluorescein Labeled protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-192. The Fluoresc 100

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1438: Influenza A virus infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[NP] Nucleoprotein (Nucleocapsid protein) (Protein N)
[N] Nucleoprotein (EC 3.1.13.-) (Nucleocapsid protein) (Protein N)
[N NP] Nucleoprotein (Nucleocapsid protein) (NP) (Protein N)
[N Segment S] Nucleoprotein (EC 3.1.13.-) (Nucleocapsid protein) (Protein N)
[N 9a] Nucleoprotein (Nucleocapsid protein) (NC) (Protein N)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro-pol] Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro] Gag-Pro polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease (EC 3.4.23.-)]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[gag-pro-pol] Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pro] Gag-Pro polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease (EC 3.4.23.-)]
[gag] Gag polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein p14]
[gag] Gag polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein p14]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[gag] Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-Pol (NC-pol); Protease (PR) (EC 3.4.23.-) (p14); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (p80); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (p46)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

Bibliography :
[30634979] Identification and localization of Tospovirus genus-wide conserved residues in 3D models of the nucleocapsid and the silencing suppressor proteins.
[30541588] Combined use of ELISA and Western blot with recombinant N protein is a powerful tool for the immunodiagnosis of avian infectious bronchitis.
[30518406] First demonstration of the circulation of a pneumovirus in French pigs by detection of anti-swine orthopneumovirus nucleoprotein antibodies.
[30333622] Cryo-EM structure of the Ebola virus nucleoprotein-RNA complex at 3.6 Å resolution.
[30217825] Human T-cell leukemia virus type 1 Gag domains have distinct RNA-binding specificities with implications for RNA packaging and dimerization.
[30108178] Highly efficient cellular uptake of a cell-penetrating peptide (CPP) derived from the capsid protein of porcine circovirus type 2.
[30056211] Binding of host factors to stabilized HIV-1 capsid tubes.
[30001425] DDX3 suppresses type I interferons and favors viral replication during Arenavirus infection.
[29996845] The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.
[29976753] -Methyladenosine-binding proteins suppress HIV-1 infectivity and viral production.