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Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; 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.-.-)]

 POL_HTLV2               Reviewed;        1461 AA.
P03363;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-DEC-2017, entry version 139.
RecName: Full=Gag-Pro-Pol polyprotein;
AltName: Full=Pr160Gag-Pro-Pol;
Contains:
RecName: Full=Matrix protein p19;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p15-pro;
Short=NC';
Short=NC-pro;
Contains:
RecName: Full=Protease;
Short=PR;
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=p1;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000305|PubMed:8623556};
EC=3.1.-.- {ECO:0000305|PubMed:8623556};
Name=gag-pro-pol;
Human T-cell leukemia virus 2 (HTLV-2).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11909;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
Chen I.S.Y., Miwa M., Sugimura T.;
"Complete nucleotide sequence of an infectious clone of human T-cell
leukemia virus type II: an open reading frame for the protease gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=2467996;
Mador N., Panet A., Honigman A.;
"Translation of gag, pro, and pol gene products of human T-cell
leukemia virus type 2.";
J. Virol. 63:2400-2404(1989).
[3]
RIBOSOMAL FRAMESHIFT.
PubMed=8371359;
Falk H., Mador N., Udi R., Panet A., Honigman A.;
"Two cis-acting signals control ribosomal frameshift between human T-
cell leukemia virus type II gag and pro genes.";
J. Virol. 67:6273-6277(1993).
[4]
FUNCTION (INTEGRASE).
PubMed=8623556; DOI=10.1006/viro.1996.0224;
Balakrishnan M., Zastrow D., Jonsson C.B.;
"Catalytic activities of the human T-cell leukemia virus type II
integrase.";
Virology 219:77-86(1996).
[5]
RIBOSOMAL FRAMESHIFT.
PubMed=11222762; DOI=10.1093/nar/29.5.1125;
Kim Y.-G., Maas S., Rich A.;
"Comparative mutational analysis of cis-acting RNA signals for
translational frameshifting in HIV-1 and HTLV-2.";
Nucleic Acids Res. 29:1125-1131(2001).
[6]
STRUCTURE BY NMR OF 1-136.
PubMed=9000634; DOI=10.1006/jmbi.1996.0700;
Christensen A.M., Massiah M.A., Turner B.G., Sundquist W.I.,
Summers M.F.;
"Three-dimensional structure of the HTLV-II matrix protein and
comparative analysis of matrix proteins from the different classes of
pathogenic human retroviruses.";
J. Mol. Biol. 264:1117-1131(1996).
-!- FUNCTION: Gag-Pro-Pol polyprotein: The matrix domain targets Gag,
Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
multipartite membrane binding signal, that includes its
myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Matrix protein p19: Matrix protein.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Capsid protein p24: Forms the spherical core of the
virus that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03362}.
-!- FUNCTION: Nucleocapsid protein p15-pro: Binds strongly to viral
nucleic acids and promote their aggregation. Also destabilizes the
nucleic acids duplexes via highly structured zinc-binding motifs.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Protease: The aspartyl protease mediates proteolytic
cleavages of Gag and Gag-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell (Potential). Cleaves the translation initiation factor eIF4G
leading to the inhibition of host cap-dependent translation (By
similarity). {ECO:0000250|UniProtKB:P03362, ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: RT is a
multifunctional enzyme that converts the viral RNA genome into
dsDNA in the cytoplasm, shortly after virus entry into the cell.
This enzyme displays a DNA polymerase activity that can copy
either DNA or RNA templates, and a ribonuclease H (RNase H)
activity that cleaves the RNA strand of RNA-DNA heteroduplexes in
a partially processive 3' to 5'-endonucleasic mode. Conversion of
viral genomic RNA into dsDNA requires many steps. A tRNA-Pro binds
to the primer-binding site (PBS) situated at the 5'-end of the
viral RNA. RT uses the 3' end of the tRNA primer to perform a
short round of RNA-dependent minus-strand DNA synthesis. The
reading proceeds through the U5 region and ends after the repeated
(R) region which is present at both ends of viral RNA. The portion
of the RNA-DNA heteroduplex is digested by the RNase H, resulting
in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA
hybridizes with the identical R region situated at the 3' end of
viral RNA. This template exchange, known as minus-strand DNA
strong stop transfer, can be either intra- or intermolecular. RT
uses the 3' end of this newly synthesized short ssDNA to perform
the RNA-dependent minus-strand DNA synthesis of the whole
template. RNase H digests the RNA template except for a polypurine
tract (PPT) situated at the 5' end of the genome. It is not clear
if both polymerase and RNase H activities are simultaneous. RNase
H probably can proceed both in a polymerase-dependent (RNA cut
into small fragments by the same RT performing DNA synthesis) and
a polymerase-independent mode (cleavage of remaining RNA fragments
by free RTs). Secondly, RT performs DNA-directed plus-strand DNA
synthesis using the PPT that has not been removed by RNase H as
primer. PPT and tRNA primers are then removed by RNase H. The 3'
and 5' ssDNA PBS regions hybridize to form a circular dsDNA
intermediate. Strand displacement synthesis by RT to the PBS and
PPT ends produces a blunt ended, linear dsDNA copy of the viral
genome that includes long terminal repeats (LTRs) at both ends (By
similarity). {ECO:0000250}.
-!- FUNCTION: Integrase: Catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. {ECO:0000305|PubMed:8623556}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
Note=The RT polymerase active site binds 2 magnesium ions.
{ECO:0000255|PROSITE-ProRule:PRU00405};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- SUBUNIT: Gag-Pro-Pol polyprotein: Homodimer; the homodimers are
part of the immature particles. Gag-Pro-Pol polyprotein: Interacts
with human TSG101 and NEDD4; these interactions are essential for
budding and release of viral particles. Matrix protein p19:
Homodimer; further assembles as homohexamers.
{ECO:0000250|UniProtKB:P03345}.
-!- INTERACTION:
O14770:MEIS2 (xeno); NbExp=3; IntAct=EBI-9676133, EBI-2804934;
-!- SUBCELLULAR LOCATION: Matrix protein p19: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p15-pro: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein. {ECO:0000305};
Name=Gag-Pro-Pol polyprotein;
IsoId=P03363-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the gag-pol genes
boundary. {ECO:0000269|PubMed:11222762,
ECO:0000269|PubMed:2467996, ECO:0000269|PubMed:8371359};
Name=Gag-Pro polyprotein;
IsoId=P03353-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the gag-pro genes
boundary. {ECO:0000269|PubMed:11222762,
ECO:0000269|PubMed:2467996, ECO:0000269|PubMed:8371359};
Name=Gag polyprotein;
IsoId=P03346-1; Sequence=External;
Note=Produced by conventional translation.
{ECO:0000269|PubMed:11222762, ECO:0000269|PubMed:2467996,
ECO:0000269|PubMed:8371359};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Matrix protein p19 contains two L
domains: a PTAP/PSAP motif which interacts with the UEV domain of
TSG101, and a PPXY motif which binds to the WW domains of the
ubiquitin ligase NEDD4. {ECO:0000250|UniProtKB:P03345}.
-!- DOMAIN: Capsid protein p24: The capsid protein N-terminus seems to
be involved in Gag-Gag interactions.
{ECO:0000250|UniProtKB:P03362}.
-!- PTM: Matrix protein p19: Phosphorylation of the matrix protein p19
by MAPK1 seems to play a role in budding.
{ECO:0000250|UniProtKB:P03345}.
-!- PTM: Gag-Pro-Pol polyprotein: Myristoylated. Myristoylation of the
matrix (MA) domain mediates the transport and binding of Gag
polyproteins to the host plasma membrane and is required for the
assembly of viral particles. {ECO:0000250|UniProtKB:P03345}.
-!- PTM: Gag-Pro-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins. The polyprotein is cleaved
during and after budding, this process is termed maturation. The
protease is autoproteolytically processed at its N- and C-termini.
{ECO:0000250|UniProtKB:P03362}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template swiching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
ProRule:PRU00405}.
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EMBL; M10060; AAB59885.1; ALT_SEQ; Genomic_DNA.
PIR; A03962; GNLJH2.
RefSeq; NP_041003.3; NC_001488.1.
PDB; 1JVR; NMR; -; A=1-136.
PDBsum; 1JVR; -.
ProteinModelPortal; P03363; -.
SMR; P03363; -.
IntAct; P03363; 8.
PRIDE; P03363; -.
GeneID; 1491941; -.
KEGG; vg:1491941; -.
OrthoDB; VOG09000135; -.
EvolutionaryTrace; P03363; -.
Proteomes; UP000009254; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR036989; D_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
InterPro; IPR017856; Integrase-like_N.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02228; Gag_p19; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Complete proteome;
DNA integration; DNA recombination; DNA-binding; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus;
Host gene expression shutoff by virus; Host-virus interaction;
Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Protease; Reference proteome; Repeat; Ribosomal frameshifting;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral nucleoprotein; Virion; Virus entry into host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 1461 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000085472.
CHAIN 2 136 Matrix protein p19.
/FTId=PRO_0000259946.
CHAIN 137 350 Capsid protein p24.
/FTId=PRO_0000259947.
CHAIN 351 446 Nucleocapsid protein p15-pro.
/FTId=PRO_0000259948.
CHAIN 447 571 Protease.
/FTId=PRO_0000261318.
PEPTIDE 572 579 p1.
/FTId=PRO_0000259949.
CHAIN 580 1166 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000259950.
CHAIN 1167 1461 Integrase.
/FTId=PRO_0000259951.
DOMAIN 473 551 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 612 802 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1029 1164 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1218 1387 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 361 378 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 384 401 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
DNA_BIND 1392 1441 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
MOTIF 94 97 PTAP/PSAP motif.
MOTIF 124 127 PPXY motif.
{ECO:0000250|UniProtKB:P03345}.
MOTIF 130 133 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P03345}.
COMPBIAS 94 150 Pro-rich.
COMPBIAS 453 456 Poly-Gln.
COMPBIAS 585 588 Poly-Pro.
ACT_SITE 478 478 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 678 678 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 753 753 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 754 754 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1038 1038 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1073 1073 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1095 1095 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1156 1156 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1229 1229 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1286 1286 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
SITE 136 137 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 350 351 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 446 447 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 571 572 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 579 580 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 1019 1020 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 1166 1167 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
STRAND 2 9 {ECO:0000244|PDB:1JVR}.
HELIX 21 33 {ECO:0000244|PDB:1JVR}.
TURN 40 42 {ECO:0000244|PDB:1JVR}.
HELIX 43 54 {ECO:0000244|PDB:1JVR}.
TURN 60 63 {ECO:0000244|PDB:1JVR}.
TURN 65 67 {ECO:0000244|PDB:1JVR}.
HELIX 68 71 {ECO:0000244|PDB:1JVR}.
HELIX 80 88 {ECO:0000244|PDB:1JVR}.
TURN 89 91 {ECO:0000244|PDB:1JVR}.
STRAND 99 103 {ECO:0000244|PDB:1JVR}.
STRAND 117 119 {ECO:0000244|PDB:1JVR}.
SEQUENCE 1461 AA; 162402 MW; 2D2911076BDD1002 CRC64;
MGQIHGLSPT PIPKAPRGLS THHWLNFLQA AYRLQPRPSD FDFQQLRRFL KLALKTPIWL
NPIDYSLLAS LIPKGYPGRV VEIINILVKN QVSPSAPAAP VPTPICPTTT PPPPPPPSPE
AHVPPPYVEP TTTQCFPILH PPGAPSAHRP WQMKDLQAIK QEVSSSALGS PQFMQTLRLA
VQQFDPTAKD LQDLLQYLCS SLVVSLHHQQ LNTLITEAET RGMTGYNPMA GPLRMQANNP
AQQGLRREYQ NLWLAAFSTL PGNTRDPSWA AILQGLEEPY CAFVERLNVA LDNGLPEGTP
KEPILRSLAY SNANKECQKI LQARGHTNSP LGEMLRTCQA WTPKDKTKVL VVQPRRPPPT
QPCFRCGKVG HWSRDCTQPR PPPGPCPLCQ DPSHWKRDCP QLKPPQEEGE PLLLDLPSTS
GTTEEKNLLK GGDLISPHPD QDISILPLIP LRQQQQPILG VRISVMGQTP QPTQALLDTG
ADLTVIPQTL VPGPVKLHDT LILGASGQTN TQFKLLQTPL HIFLPFRRSP VILSSCLLDT
HNKWTIIGRD ALQQCQGLLY LPDDPSPHQL LPIATPNTIG LEHLPPPPQV DQFPLNLPER
LQALNDLVSK ALEAGHIEPY SGPGNNPVFP VKKPNGKWRF IHDLRATNAI TTTLTSPSPG
PPDLTSLPTA LPHLQTIDLT DAFFQIPLPK QYQPYFAFTI PQPCNYGPGT RYAWTVLPQG
FKNSPTLFEQ QLAAVLNPMR KMFPTSTIVQ YMDDILLASP TNEELQQLSQ LTLQALTTHG
LPISQEKTQQ TPGQIRFLGQ VISPNHITYE STPTIPIKSQ WTLTELQVIL GEIQWVSKGT
PILRKHLQSL YSALHGYRDP RACITLTPQQ LHALHAIQQA LQHNCRGRLN PALPLLGLIS
LSTSGTTSVI FQPKQNWPLA WLHTPHPPTS LCPWGHLLAC TILTLDKYTL QHYGQLCQSF
HHNMSKQALC DFLRNSPHPS VGILIHHMGR FHNLGSQPSG PWKTLLHLPT LLQEPRLLRP
IFTLSPVVLD TAPCLFSDGS PQKAAYVLWD QTILQQDITP LPSHETHSAQ KGELLALICG
LRAAKPWPSL NIFLDSKYLI KYLHSLAIGA FLGTSAHQTL QAALPPLLQG KTIYLHHVRS
HTNLPDPIST FNEYTDSLIL APLVPLTPQG LHGLTHCNQR ALVSFGATPR EAKSLVQTCH
TCQTINSQHH MPRGYIRRGL LPNHIWQGDV THYKYKKYKY CLHVWVDTFS GAVSVSCKKK
ETSCETISAV LQAISLLGKP LHINTDNGPA FLSQEFQEFC TSYRIKHSTH IPYNPTSSGL
VERTNGVIKN LLNKYLLDCP NLPLDNAIHK ALWTLNQLNV MNPSGKTRWQ IHHSPPLPPI
PEASTPPKPP PKWFYYKLPG LTNQRWKGPL QSLQEAAGAA LLSIDGSPRW IPWRFLKKAA
CPRPDASELA EHAATDHQHH G


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PCR-505S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10units
PCR-505L SCRIPT Reverse Transcriptase, L pack Reverse Transcriptase with increased thermal stability 50kunits
PCR-505L SCRIPT Reverse Transcriptase, L pack Reverse Transcriptase with increased thermal stability 50000 units
PCR-505L SCRIPT Reverse Transcriptase, L pack Reverse Transcriptase with increased thermal stability 50000units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10000 units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10000units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10kunits
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
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
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
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
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
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
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
PCR-501S M_MLV Reverse Transcriptase (RNase H_), S pack Reverse Transcriptase 10000units
PCR-501L M_MLV Reverse Transcriptase (RNase H_), L pack Reverse Transcriptase 50000units
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
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
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


 

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