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Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-Gag (NC-gag)]

 GAG_MLVMS               Reviewed;         538 AA.
P03332; Q9WJP4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-JUN-2018, entry version 141.
RecName: Full=Gag polyprotein;
Short=Pr65gag;
AltName: Full=Core polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10-Gag;
Short=NC-gag;
Name=gag;
Moloney murine leukemia virus (isolate Shinnick) (MoMLV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; Murine leukemia virus.
NCBI_TaxID=928306;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE PMLV-1).
PubMed=6169994; DOI=10.1038/293543a0;
Shinnick T.M., Lerner R.A., Sutcliffe J.G.;
"Nucleotide sequence of Moloney murine leukaemia virus.";
Nature 293:543-548(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Chappey C.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-31, AND MYRISTOYLATION AT GLY-2.
PubMed=6340098; DOI=10.1073/pnas.80.2.339;
Henderson L.E., Krutzsch H.C., Oroszlan S.;
"Myristyl amino-terminal acylation of murine retrovirus proteins: an
unusual post-translational proteins modification.";
Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983).
[4]
PROTEIN SEQUENCE OF 479-529.
PubMed=6267042;
Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W.,
Oroszlan S.;
"Primary structure of the low molecular weight nucleic acid-binding
proteins of murine leukemia viruses.";
J. Biol. Chem. 256:8400-8406(1981).
[5]
SUBCELLULAR LOCATION (GAG POLYPROTEIN).
PubMed=8991095;
Suomalainen M., Hultenby K., Garoff H.;
"Targeting of Moloney murine leukemia virus gag precursor to the site
of virus budding.";
J. Cell Biol. 135:1841-1852(1996).
[6]
SUBUNIT (CAPSID PROTEIN P30).
PubMed=12093170;
Mayo K., McDermott J., Barklis E.;
"Hexagonal organization of Moloney murine leukemia virus capsid
proteins.";
Virology 298:30-38(2002).
[7]
PHOSPHORYLATION AT SER-192, AND MUTAGENESIS OF SER-137; SER-148;
SER-150; SER-192; SER-196; SER-209 AND SER-212.
PubMed=12525616; DOI=10.1128/JVI.77.3.1820-1829.2003;
Yueh A., Goff S.P.;
"Phosphorylated serine residues and an arginine-rich domain of the
moloney murine leukemia virus p12 protein are required for early
events of viral infection.";
J. Virol. 77:1820-1829(2003).
[8]
INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX (GAG
POLYPROTEIN), AND MUTAGENESIS OF TYR-165.
PubMed=15908698; DOI=10.1074/jbc.M413735200;
Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R.,
Bertrand E., Basyuk E.;
"Tsg101 and Alix interact with murine leukemia virus Gag and cooperate
with Nedd4 ubiquitin ligases during budding.";
J. Biol. Chem. 280:27004-27012(2005).
[9]
INTERACTION WITH UBE2I AND PIAS4 (CAPSID PROTEIN P30), AND SUMOYLATION
(CAPSID PROTEIN P30).
PubMed=16352559; DOI=10.1128/JVI.80.1.342-352.2006;
Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K.,
Pu S.-Y., Goff S.P.;
"Interaction of moloney murine leukemia virus capsid with Ubc9 and
PIASy mediates SUMO-1 addition required early in infection.";
J. Virol. 80:342-352(2006).
[10]
PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
PubMed=16603535; DOI=10.1099/vir.0.81382-0;
Feher A., Boross P., Sperka T., Miklossy G., Kadas J., Bagossi P.,
Oroszlan S., Weber I.T., Tozser J.;
"Characterization of the murine leukemia virus protease and its
comparison with the human immunodeficiency virus type 1 protease.";
J. Gen. Virol. 87:1321-1330(2006).
[11]
FUNCTION (RNA-BINDING PHOSPHOPROTEIN P12), AND SUBCELLULAR LOCATION
(RNA-BINDING PHOSPHOPROTEIN P12).
PubMed=21085616; DOI=10.1371/journal.ppat.1001183;
Prizan-Ravid A., Elis E., Laham-Karam N., Selig S., Ehrlich M.,
Bacharach E.;
"The Gag cleavage product, p12, is a functional constituent of the
murine leukemia virus pre-integration complex.";
PLoS Pathog. 6:E1001183-E1001183(2010).
[12]
DOMAIN LATE-BUDDING, FUNCTION (GAG POLYPROTEIN), AND UBIQUITINATION
(GAG POLYPROTEIN).
PubMed=19864377; DOI=10.1128/JVI.01319-09;
Jadwin J.A., Rudd V., Sette P., Challa S., Bouamr F.;
"Late domain-independent rescue of a release-deficient Moloney murine
leukemia virus by the ubiquitin ligase Itch.";
J. Virol. 84:704-715(2010).
[13]
FUNCTION (RNA-BINDING PHOSPHOPROTEIN P12), SUBCELLULAR LOCATION
(RNA-BINDING PHOSPHOPROTEIN P12), AND MUTAGENESIS OF SER-192 AND
SER-196.
PubMed=23300449; DOI=10.1371/journal.ppat.1003103;
Elis E., Ehrlich M., Prizan-Ravid A., Laham-Karam N., Bacharach E.;
"p12 tethers the murine leukemia virus pre-integration complex to
mitotic chromosomes.";
PLoS Pathog. 8:E1003103-E1003103(2012).
[14]
STRUCTURE BY NMR OF 492-531.
PubMed=8019131; DOI=10.1007/BF00175244;
Demene H., Jullian N., Morellet N., de Rocquigny H., Cornille F.,
Maigret B., Roques B.P.;
"Three-dimensional 1H NMR structure of the nucleocapsid protein NCp10
of Moloney murine leukemia virus.";
J. Biomol. NMR 4:153-170(1994).
[15]
STRUCTURE BY NMR OF 352-382.
PubMed=9799104; DOI=10.1046/j.1432-1327.1998.2570069.x;
Clish C.B., Peyton D.H., Barklis E.;
"Solution structures of human immunodeficiency virus type 1 (HIV-1)
and moloney murine leukemia virus (MoMLV) capsid protein major-
homology-region peptide analogs by NMR spectroscopy.";
Eur. J. Biochem. 257:69-77(1998).
[16]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1-99, AND FUNCTION (MATRIX
PROTEIN P15).
PubMed=12467570; DOI=10.1016/S0969-2126(02)00896-1;
Riffel N., Harlos K., Iourin O., Rao Z., Kingsman A., Stuart D.,
Fry E.;
"Atomic resolution structure of Moloney murine leukemia virus matrix
protein and its relationship to other retroviral matrix proteins.";
Structure 10:1627-1636(2002).
[17]
STRUCTURE BY NMR OF 479-534, FUNCTION (NUCLEOCAPSID PROTEIN P10-GAG),
AND RNA-BINDING (NUCLEOCAPSID PROTEIN P10-GAG).
PubMed=15457265; DOI=10.1038/nature02944;
D'Souza V., Summers M.F.;
"Structural basis for packaging the dimeric genome of Moloney murine
leukaemia virus.";
Nature 431:586-590(2004).
[18]
STRUCTURE BY NMR OF 479-534, AND RNA-BINDING (NUCLEOCAPSID PROTEIN
P10-GAG).
PubMed=15751950; DOI=10.1021/bi047639q;
Dey A., York D., Smalls-Mantey A., Summers M.F.;
"Composition and sequence-dependent binding of RNA to the nucleocapsid
protein of Moloney murine leukemia virus.";
Biochemistry 44:3735-3744(2005).
-!- FUNCTION: Gag polyprotein: Plays a role in budding and is
processed by the viral protease during virion maturation outside
the cell. During budding, it recruits, in a PPXY-dependent or
independent manner, Nedd4-like ubiquitin ligases that conjugate
ubiquitin molecules to Gag, or to Gag binding host factors.
Interaction with HECT ubiquitin ligases probably links the viral
protein to the host ESCRT pathway and facilitates release.
{ECO:0000269|PubMed:19864377}.
-!- FUNCTION: Matrix protein p15: Targets Gag and gag-pol polyproteins
to the plasma membrane via a multipartite membrane binding signal,
that includes its myristoylated N-terminus. Also mediates nuclear
localization of the pre-integration complex.
{ECO:0000305|PubMed:12467570}.
-!- FUNCTION: RNA-binding phosphoprotein p12: Constituent of the pre-
integration complex (PIC) which tethers the latter to mitotic
chromosomes. {ECO:0000269|PubMed:21085616,
ECO:0000269|PubMed:23300449}.
-!- FUNCTION: Capsid protein p30: Forms the spherical core of the
virion that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03336}.
-!- FUNCTION: Nucleocapsid protein p10-Gag: Involved in the packaging
and encapsidation of two copies of the genome. Binds with high
affinity to conserved UCUG elements within the packaging signal,
located near the 5'-end of the genome. This binding is dependent
on genome dimerization. {ECO:0000269|PubMed:15457265}.
-!- SUBUNIT: Capsid protein p30: Homohexamer; further associates as
homomultimer (By similarity). Capsid protein p30: The virus core
is composed of a lattice formed from hexagonal rings, each
containing six capsid monomers (PubMed:12093170). Capsid protein
p30: Interacts with mouse UBE2I and mouse PIAS4. Gag polyprotein:
Interacts (via PPXY motif) with host NEDD4 (PubMed:15908698). Gag
polyprotein: Interacts (via PSAP motif) with host TSG101
(PubMed:15908698). Gag polyprotein: Interacts (via LYPX(n)L motif)
with host PDCD6IP (PubMed:15908698).
{ECO:0000250|UniProtKB:P03336, ECO:0000269|PubMed:12093170,
ECO:0000269|PubMed:15908698, ECO:0000269|PubMed:16352559}.
-!- INTERACTION:
Q9QZK7:Dok3 (xeno); NbExp=3; IntAct=EBI-935477, EBI-2906753;
Q9JKF1:Iqgap1 (xeno); NbExp=17; IntAct=EBI-935477, EBI-644633;
-!- SUBCELLULAR LOCATION: Gag polyprotein: Virion {ECO:0000305}. Host
cell membrane {ECO:0000269|PubMed:8991095}; Lipid-anchor
{ECO:0000305}. Host late endosome membrane {ECO:0000305}; Lipid-
anchor {ECO:0000305}. Host endosome, host multivesicular body
{ECO:0000250|UniProtKB:P26807}. Note=These locations are probably
linked to virus assembly sites. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p30: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p10-Gag: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-binding phosphoprotein p12: Host
cytoplasm {ECO:0000269|PubMed:21085616,
ECO:0000269|PubMed:23300449}. Note=Localizes to the host cytoplasm
early in infection and binds to the mitotic chromosomes later on.
{ECO:0000269|PubMed:23300449}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Pr65gag;
IsoId=P03332-1; Sequence=Displayed;
Name=Pr80gag; Synonyms=GlycoGag;
IsoId=P03332-2; Sequence=Not described;
Note=Produced by an upstream CUG initiation codon.
{ECO:0000305};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins. RNA-
binding phosphoprotein p12 contains one L domain: a PPXY motif
which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase.
PPXY motif is essential for virus egress. Matrix protein p15
contains one L domain: a PTAP/PSAP motif, which interacts with the
UEV domain of TSG101. The junction between the matrix protein p15
and RNA-binding phosphoprotein p12 also contains one L domain: a
LYPX(n)L motif which interacts with PDCD6IP. Both PSAP and
LYPX(n)L domains might play little to no role in budding and
possibly drive residual virus release.
{ECO:0000269|PubMed:19864377}.
-!- PTM: Gag polyprotein: Ubiquitinated by ITCH. Gag can recruit the
ubiquitin ligase Itch in an L domain-independent manner to
facilitate virus release via a mechanism that involves Gag
ubiquitination. {ECO:0000269|PubMed:19864377}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages by the viral
protease yield mature proteins. The protease is released by
autocatalytic cleavage. The polyprotein is cleaved during and
after budding, this process is termed maturation.
{ECO:0000269|PubMed:16603535}.
-!- PTM: Capsid protein p30: Sumoylated; required for virus
replication. {ECO:0000269|PubMed:16352559}.
-!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
residues. {ECO:0000269|PubMed:12525616}.
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EMBL; J02255; AAB59942.1; -; Genomic_RNA.
EMBL; AF033811; AAC82566.1; -; Genomic_RNA.
PIR; A03930; FOMV1M.
RefSeq; NP_057934.1; NC_001501.1.
PDB; 1A6B; NMR; -; B=492-531.
PDB; 1BM4; NMR; -; A=352-382.
PDB; 1MN8; X-ray; 1.00 A; A/B/C/D=1-99.
PDB; 1U6P; NMR; -; A=479-534.
PDB; 1WWD; NMR; -; A=479-534.
PDB; 1WWE; NMR; -; A=479-534.
PDB; 1WWF; NMR; -; A=479-534.
PDB; 1WWG; NMR; -; A=479-534.
PDBsum; 1A6B; -.
PDBsum; 1BM4; -.
PDBsum; 1MN8; -.
PDBsum; 1U6P; -.
PDBsum; 1WWD; -.
PDBsum; 1WWE; -.
PDBsum; 1WWF; -.
PDBsum; 1WWG; -.
ProteinModelPortal; P03332; -.
SMR; P03332; -.
IntAct; P03332; 6.
MINT; P03332; -.
iPTMnet; P03332; -.
GeneID; 1491870; -.
KEGG; vg:1491870; -.
OrthoDB; VOG090000NB; -.
EvolutionaryTrace; P03332; -.
Proteomes; UP000006625; Genome.
Proteomes; UP000180702; Genome.
GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR036946; G_retro_matrix_sf.
InterPro; IPR002079; Gag_p12.
InterPro; IPR003036; Gag_P30.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF01141; Gag_p12; 1.
Pfam; PF02093; Gag_p30; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Capsid protein; Coiled coil;
Complete proteome; Direct protein sequencing; Host cell membrane;
Host cytoplasm; Host endosome; Host membrane; Host-virus interaction;
Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
Reference proteome; RNA-binding; Ubl conjugation; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255,
ECO:0000269|PubMed:6340098}.
CHAIN 2 538 Gag polyprotein.
/FTId=PRO_0000390815.
CHAIN 2 131 Matrix protein p15.
/FTId=PRO_0000040912.
CHAIN 132 215 RNA-binding phosphoprotein p12.
/FTId=PRO_0000040913.
CHAIN 216 478 Capsid protein p30.
/FTId=PRO_0000040914.
CHAIN 479 538 Nucleocapsid protein p10-Gag.
/FTId=PRO_0000040915.
ZN_FING 502 519 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 345 393 Interaction with host PIAS4.
{ECO:0000269|PubMed:16352559}.
REGION 430 435 Interaction with host UBE2I.
{ECO:0000269|PubMed:16352559}.
COILED 438 478 {ECO:0000255}.
MOTIF 111 114 PTAP/PSAP motif.
{ECO:0000269|PubMed:19864377}.
MOTIF 130 134 LYPX(n)L motif.
{ECO:0000269|PubMed:19864377}.
MOTIF 162 165 PPXY motif.
{ECO:0000269|PubMed:19864377}.
COMPBIAS 71 193 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
SITE 131 132 Cleavage; by viral protease.
{ECO:0000269|PubMed:16603535}.
SITE 215 216 Cleavage; by viral protease.
{ECO:0000269|PubMed:16603535}.
SITE 478 479 Cleavage; by viral protease.
{ECO:0000269|PubMed:16603535}.
MOD_RES 192 192 Phosphoserine; by host.
{ECO:0000305|PubMed:12525616}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255,
ECO:0000269|PubMed:6340098}.
MUTAGEN 114 114 P->A: Slight reduction in the number of
virus-like particles produced.
MUTAGEN 137 137 S->A: No effect on reverse transcription
activity. {ECO:0000269|PubMed:12525616}.
MUTAGEN 148 148 S->A: No effect on reverse transcription
activity; when associated with A-150.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 150 150 S->A: No effect on reverse transcription
activity; when associated with A-148.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 165 165 Y->A: Drastic reduction in the number of
virus-like particles produced.
{ECO:0000269|PubMed:15908698}.
MUTAGEN 192 192 S->A: Complete loss of reverse
transcription activity.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 192 192 S->A: Complete loss of stable anchoring
of viral PIC to mitotic chromosomes; when
associated with A-196.
{ECO:0000269|PubMed:23300449}.
MUTAGEN 192 192 S->D: Complete loss of reverse
transcription activity.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 196 196 S->A: Complete loss of stable anchoring
of viral PIC to mitotic chromosomes; when
associated with A-192.
{ECO:0000269|PubMed:23300449}.
MUTAGEN 196 196 S->A: No effect on reverse transcription
activity. {ECO:0000269|PubMed:12525616}.
MUTAGEN 209 209 S->A: Strongly reduced reverse
transcription activity.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 209 209 S->D: Strongly reduced reverse
transcription activity.
{ECO:0000269|PubMed:12525616}.
MUTAGEN 212 212 S->A: No effect on reverse transcription
activity. {ECO:0000269|PubMed:12525616}.
HELIX 8 14 {ECO:0000244|PDB:1MN8}.
HELIX 16 25 {ECO:0000244|PDB:1MN8}.
HELIX 32 40 {ECO:0000244|PDB:1MN8}.
HELIX 43 46 {ECO:0000244|PDB:1MN8}.
HELIX 58 68 {ECO:0000244|PDB:1MN8}.
HELIX 77 79 {ECO:0000244|PDB:1MN8}.
HELIX 80 91 {ECO:0000244|PDB:1MN8}.
TURN 356 360 {ECO:0000244|PDB:1BM4}.
HELIX 361 363 {ECO:0000244|PDB:1BM4}.
HELIX 364 378 {ECO:0000244|PDB:1BM4}.
STRAND 494 496 {ECO:0000244|PDB:1WWD}.
STRAND 501 503 {ECO:0000244|PDB:1A6B}.
STRAND 505 507 {ECO:0000244|PDB:1A6B}.
STRAND 510 512 {ECO:0000244|PDB:1U6P}.
HELIX 514 516 {ECO:0000244|PDB:1U6P}.
STRAND 518 520 {ECO:0000244|PDB:1A6B}.
STRAND 522 524 {ECO:0000244|PDB:1WWG}.
SEQUENCE 538 AA; 60858 MW; 8A7652439B464495 CRC64;
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP
PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT
VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDD


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EIAAB13041 Endogenous retrovirus group W member 1,Envelope polyprotein gPr73,Enverin,Env-W,ERVW-1,ERVWE1,HERV-7q Envelope protein,HERV-W envelope protein,HERV-W_7q21.2 provirus ancestral Env polyprotein,Homo sap
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
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
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
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
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
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
orb81566 Hepatitis Virus Nucleocapsid (core), Horseradish Peroxidase Labled protein The E.coli derived recombinant HRP Labeled protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-1 100
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
orb81573 Hepatitis Virus Nucleocapsid (core) 22kDa, Rhodamine Labeled protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-192. The Rhodamine 100
EIAAB12959 Envelope polyprotein,ERVK5,HERV-K(II) envelope protein,HERV-K_3q12.3 provirus ancestral Env polyprotein,Homo sapiens,Human
E0052h ELISA Homo sapiens,Human,IBP1,IBP-1,IGF-binding protein 1,IGFBP1,IGFBP-1,Insulin-like growth factor-binding protein 1,Placental protein 12,PP12 96T
E0052h ELISA kit Homo sapiens,Human,IBP1,IBP-1,IGF-binding protein 1,IGFBP1,IGFBP-1,Insulin-like growth factor-binding protein 1,Placental protein 12,PP12 96T


 

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