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

Protein Vpr (R ORF protein) (Viral protein R)

 VPR_HV1H2               Reviewed;          96 AA.
P69726; P05926; Q85577;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
04-FEB-2015, sequence version 2.
20-DEC-2017, entry version 85.
RecName: Full=Protein Vpr {ECO:0000255|HAMAP-Rule:MF_04080};
AltName: Full=R ORF protein {ECO:0000255|HAMAP-Rule:MF_04080};
AltName: Full=Viral protein R {ECO:0000255|HAMAP-Rule:MF_04080};
Name=vpr {ECO:0000255|HAMAP-Rule:MF_04080};
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11706;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3040055; DOI=10.1089/aid.1987.3.57;
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
"Complete nucleotide sequences of functional clones of the AIDS
virus.";
AIDS Res. Hum. Retroviruses 3:57-69(1987).
[2]
FUNCTION.
STRAIN=isolate BRU/LAI;
PubMed=2136707;
Cohen E.A., Terwilliger E.F., Jalinoos Y., Proulx J., Sodroski J.G.,
Haseltine W.A.;
"Identification of HIV-1 vpr product and function.";
J. Acquir. Immune Defic. Syndr. 3:11-18(1990).
[3]
SUBCELLULAR LOCATION.
STRAIN=isolate BRU/LAI;
PubMed=2139896;
Cohen E.A., Dehni G., Sodroski J.G., Haseltine W.A.;
"Human immunodeficiency virus vpr product is a virion-associated
regulatory protein.";
J. Virol. 64:3097-3099(1990).
[4]
SUBCELLULAR LOCATION.
STRAIN=isolate BRU/LAI;
PubMed=8411357;
Lu Y.L., Spearman P., Ratner L.;
"Human immunodeficiency virus type 1 viral protein R localization in
infected cells and virions.";
J. Virol. 67:6542-6550(1993).
[5]
HOMOOLIGOMERIZATION.
PubMed=7798208;
Zhao L.J., Wang L., Mukherjee S., Narayan O.;
"Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated
by the N-terminal domain.";
J. Biol. Chem. 269:32131-32137(1994).
[6]
INTERACTION WITH P6-GAG.
STRAIN=isolate BRU/LAI;
PubMed=7474102;
Lu Y.L., Bennett R.P., Wills J.W., Gorelick R., Ratner L.;
"A leucine triplet repeat sequence (LXX)4 in p6gag is important for
Vpr incorporation into human immunodeficiency virus type 1
particles.";
J. Virol. 69:6873-6879(1995).
[7]
FUNCTION.
STRAIN=isolate BRU/LAI;
PubMed=7474100;
Re F., Braaten D., Franke E.K., Luban J.;
"Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2
by inhibiting the activation of p34cdc2-cyclin B.";
J. Virol. 69:6859-6864(1995).
[8]
FUNCTION.
STRAIN=isolate BRU/LAI;
PubMed=7666531;
Jowett J.B., Planelles V., Poon B., Shah N.P., Chen M.L., Chen I.S.;
"The human immunodeficiency virus type 1 vpr gene arrests infected T
cells in the G2 + M phase of the cell cycle.";
J. Virol. 69:6304-6313(1995).
[9]
INTERACTION WITH HUMAN UNG.
STRAIN=isolate BRU/LAI;
PubMed=9151883;
Selig L., Benichou S., Rogel M.E., Wu L.I., Vodicka M.A., Sire J.,
Benarous R., Emerman M.;
"Uracil DNA glycosylase specifically interacts with Vpr of both human
immunodeficiency virus type 1 and simian immunodeficiency virus of
sooty mangabeys, but binding does not correlate with cell cycle
arrest.";
J. Virol. 71:4842-4846(1997).
[10]
INTERACTION WITH HUMAN RAD23A.
STRAIN=isolate BRU/LAI;
PubMed=9371639;
Withers-Ward E.S., Jowett J.B., Stewart S.A., Xie Y.M., Garfinkel A.,
Shibagaki Y., Chow S.A., Shah N., Hanaoka F., Sawitz D.G.,
Armstrong R.W., Souza L.M., Chen I.S.;
"Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a
cellular protein implicated in nucleotide excision DNA repair.";
J. Virol. 71:9732-9742(1997).
[11]
FUNCTION.
PubMed=10518572; DOI=10.1073/pnas.96.21.12039;
Stewart S.A., Poon B., Jowett J.B., Xie Y., Chen I.S.;
"Lentiviral delivery of HIV-1 Vpr protein induces apoptosis in
transformed cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:12039-12043(1999).
[12]
FUNCTION.
PubMed=11000244; DOI=10.1128/JVI.74.20.9717-9726.2000;
Patel C.A., Mukhtar M., Pomerantz R.J.;
"Human immunodeficiency virus type 1 Vpr induces apoptosis in human
neuronal cells.";
J. Virol. 74:9717-9726(2000).
[13]
PHOSPHORYLATION AT SER-79; SER-94 AND SER-96.
STRAIN=Clone pNL4-3;
PubMed=10864665; DOI=10.1128/JVI.74.14.6520-6527.2000;
Zhou Y., Ratner L.;
"Phosphorylation of human immunodeficiency virus type 1 Vpr regulates
cell cycle arrest.";
J. Virol. 74:6520-6527(2000).
[14]
FUNCTION.
STRAIN=isolate BRU/LAI;
PubMed=12417576; DOI=10.1083/jcb.200203150;
McDonald D., Vodicka M.A., Lucero G., Svitkina T.M., Borisy G.G.,
Emerman M., Hope T.J.;
"Visualization of the intracellular behavior of HIV in living cells.";
J. Cell Biol. 159:441-452(2002).
[15]
PHOSPHORYLATION AT SER-79.
STRAIN=isolate BRU/LAI;
PubMed=11860675; DOI=10.1089/088922202753472856;
Agostini I., Popov S., Hao T., Li J.H., Dubrovsky L., Chaika O.,
Chaika N., Lewis R., Bukrinsky M.;
"Phosphorylation of Vpr regulates HIV type 1 nuclear import and
macrophage infection.";
AIDS Res. Hum. Retroviruses 18:283-288(2002).
[16]
REVIEW.
PubMed=16511342;
Moon H.S., Yang J.S.;
"Role of HIV Vpr as a regulator of apoptosis and an effector on
bystander cells.";
Mol. Cells 21:7-20(2006).
[17]
FUNCTION, AND SUBUNIT.
STRAIN=isolate BRU/LAI;
PubMed=17314515;
Le Rouzic E., Belaiedouni N., Estrabaud E., Morel M., Rain J.-C.,
Transy C., Margottin-Goguet F.;
"HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor
of the Cul4-DDB1 ubiquitin ligase.";
Cell Cycle 6:182-188(2007).
[18]
FUNCTION, AND SUBUNIT.
STRAIN=isolate BRU/LAI;
PubMed=17630831; DOI=10.1371/journal.ppat.0030085;
Belzile J.P., Duisit G., Rougeau N., Mercier J., Finzi A., Cohen E.A.;
"HIV-1 Vpr-mediated G2 arrest involves the DDB1-CUL4A[VPRBP] E3
ubiquitin ligase.";
PLoS Pathog. 3:E85-E85(2007).
[19]
FUNCTION, AND INTERACTION WITH HOST DCAF1.
STRAIN=isolate BRU/LAI;
PubMed=23612978; DOI=10.1074/jbc.M112.416735;
Wang X., Singh S., Jung H.Y., Yang G., Jun S., Sastry K.J., Park J.I.;
"HIV-1 Vpr protein inhibits telomerase activity via the EDD-DDB1-VPRBP
E3 ligase complex.";
J. Biol. Chem. 288:15474-15480(2013).
[20]
FUNCTION, AND INTERACTION WITH HOST DCAF1.
STRAIN=isolate BRU/LAI;
PubMed=24116224; DOI=10.1371/journal.pone.0077320;
Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C.,
Bouaziz S., Ramirez B.C., Margottin-Goguet F.;
"HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the
NuRD Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP.";
PLoS ONE 8:E77320-E77320(2013).
[21]
REVIEW.
PubMed=24744753; DOI=10.3389/fmicb.2014.00127;
Guenzel C.A., Herate C., Benichou S.;
"HIV-1 Vpr-a still 'enigmatic multitasker'.";
Front. Microbiol. 5:1-13(2014).
-!- FUNCTION: During virus entry, plays a role in the transport of the
viral pre-integration (PIC) complex to the host nucleus. This
function is crucial for viral infection of non-dividing
macrophages. May act directly at the nuclear pore complex, by
binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
{ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:10518572,
ECO:0000269|PubMed:12417576, ECO:0000269|PubMed:2136707}.
-!- FUNCTION: During virus replication, may deplete host UNG protein,
and incude G2-M cell cycle arrest. Acts by targeting specific host
proteins for degradation by the 26S proteasome, through
association with the cellular CUL4A-DDB1 E3 ligase complex by
direct interaction with host VPRPB/DCAF-1. Cell cycle arrest
reportedly occurs within hours of infection and is not blocked by
antiviral agents, suggesting that it is initiated by the VPR
carried into the virion. Additionally, VPR induces apoptosis in a
cell cycle dependent manner suggesting that these two effects are
mechanistically linked. Detected in the serum and cerebrospinal
fluid of AIDS patient, VPR may also induce cell death to bystander
cells. {ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:11000244, ECO:0000269|PubMed:12417576,
ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17630831,
ECO:0000269|PubMed:23612978, ECO:0000269|PubMed:24116224,
ECO:0000269|PubMed:7474100, ECO:0000269|PubMed:7666531}.
-!- SUBUNIT: Homooligomer, may form homodimer. Interacts with p6-gag
region of the Pr55 Gag precursor protein through a (Leu-X-X)4
motif near the C-terminus of the P6gag protein. Interacts with
host UNG. May interact with host RAD23A/HHR23A. Interacts with
host VPRBP/DCAF1, leading to hijack the CUL4A-RBX1-DDB1-
DCAF1/VPRBP complex, mediating ubiquitination of host proteins
such as TERT and ZGPAT and arrest of the cell cycle in G2 phase.
{ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:17314515,
ECO:0000269|PubMed:23612978, ECO:0000269|PubMed:24116224,
ECO:0000269|PubMed:7474102, ECO:0000269|PubMed:7798208,
ECO:0000269|PubMed:9151883, ECO:0000269|PubMed:9371639}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:2139896, ECO:0000269|PubMed:8411357}. Host
nucleus {ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:8411357}. Host extracellular space
{ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion
is dependent on p6 GAG sequences. Lacks a canonical nuclear
localization signal, thus import into nucleus may function
independently of the human importin pathway. Detected in high
quantity in the serum and cerebrospinal fluid of AIDS patient.
{ECO:0000255|HAMAP-Rule:MF_04080, ECO:0000269|PubMed:3040055}.
-!- PTM: Phosphorylated on several residues by host. These
phosphorylations regulate VPR activity for the nuclear import of
the HIV-1 pre-integration complex. {ECO:0000255|HAMAP-
Rule:MF_04080, ECO:0000269|PubMed:10864665,
ECO:0000269|PubMed:11860675}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K). {ECO:0000255|HAMAP-Rule:MF_04080}.
-!- SIMILARITY: Belongs to the HIV-1 VPR protein family.
{ECO:0000255|HAMAP-Rule:MF_04080}.
-!- SEQUENCE CAUTION:
Sequence=AAB50261.1; Type=Frameshift; Positions=72; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=Vpr
entry;
URL="http://www.bioafrica.net/proteomics/VPRprot.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K03455; AAB50261.1; ALT_FRAME; Genomic_RNA.
PDB; 4U1S; X-ray; 1.76 A; C=34-42.
PDBsum; 4U1S; -.
SMR; P69726; -.
IntAct; P69726; 4.
iPTMnet; P69726; -.
OrthoDB; VOG090001DK; -.
Reactome; R-HSA-162585; Uncoating of the HIV Virion.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-162592; Integration of provirus.
Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
Reactome; R-HSA-164516; Minus-strand DNA synthesis.
Reactome; R-HSA-164525; Plus-strand DNA synthesis.
Reactome; R-HSA-164843; 2-LTR circle formation.
Reactome; R-HSA-173107; Binding and entry of HIV virion.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
Reactome; R-HSA-180897; Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabilization.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Proteomes; UP000002241; Genome.
GO; GO:0043655; C:extracellular space of host; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0019012; C:virion; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030260; P:entry into host cell; TAS:Reactome.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0019051; P:induction by virus of host apoptotic process; IDA:UniProtKB.
GO; GO:0051701; P:interaction with host; IPI:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0051169; P:nuclear transport; TAS:Reactome.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome.
GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
HAMAP; MF_04080; HIV_VPR; 1.
InterPro; IPR000012; RetroV_VpR/X.
Pfam; PF00522; VPR; 1.
PRINTS; PR00444; HIVVPRVPX.
1: Evidence at protein level;
3D-structure; Activator; AIDS; Apoptosis; Cell cycle;
Complete proteome; Host G2/M cell cycle arrest by virus; Host nucleus;
Host-virus interaction; Ion channel; Ion transport;
Modulation of host cell cycle by virus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Transport; Viral penetration into host nucleus; Virion;
Virus entry into host cell.
CHAIN 1 96 Protein Vpr.
/FTId=PRO_0000085451.
REGION 1 42 Homooligomerization. {ECO:0000255|HAMAP-
Rule:MF_04080,
ECO:0000269|PubMed:7798208}.
MOD_RES 79 79 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665,
ECO:0000269|PubMed:11860675}.
MOD_RES 94 94 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665}.
MOD_RES 96 96 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04080,
ECO:0000269|PubMed:10864665}.
SEQUENCE 96 AA; 11323 MW; 42892A4249E83D3E CRC64;
MEQAPEDQGP QREPHNEWTL ELLEELKNEA VRHFPRIWLH GLGQHIYETY GDTWAGVEAI
IRILQQLLFI HFRIGCRHSR IGVTRQRRAR NGASRS


Related products :

Catalog number Product name Quantity
SCH-OBT1907X RECOMBINANT SARS MATRIX PROTEIN (aa182_216), Product Type Recombinant Protein, Specificity SARS MEMBRANE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E 1 mg
OBT1907X RECOMBINANT SARS MATRIX PROTEIN (aa182_216), Product Type Recombinant Protein, Specificity SARS MEMBRANE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E 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
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
SCH-OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
OBT1908X RECOMBINANT SARS ENVELOPE PROTEIN (aa1_76), Product Type Recombinant Protein, Specificity SARS ENVELOPE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, 1 mg
SCH-OBT1908X RECOMBINANT SARS ENVELOPE PROTEIN (aa1_76), Product Type Recombinant Protein, Specificity SARS ENVELOPE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, 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
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
SCH-OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 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
OBT1908G RECOMBINANT SARS ENVELOPE PROTEIN (aa1_76), Product Type Recombinant Protein, Specificity SARS ENVELOPE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, 0.5 mg
OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 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
SCH-OBT1908G RECOMBINANT SARS ENVELOPE PROTEIN (aa1_76), Product Type Recombinant Protein, Specificity SARS ENVELOPE PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, 0.5 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
32-106 Akt3 (also designated protein kinase B gamma or v-akt murine thymoma viral oncogene homolog 3),with 479-amino acid protein (about 53kDa), belongs to the AKT serine_threonine protein kinase family, whi 0.1 mL
32-105 Akt2 (also designated protein kinase B beta or v-akt murine thymoma viral oncogene homolog 2 ), with 481-amino acid protein (about 53kDa), belongs to the AKT serine_threonine protein kinase family, wh 0.1 mL
GWB-T00025 Rotavirus Antigen (Strain SA-11) >60 percent Viral Protein Protein
00199-V Recombinant Viral antigens, HIV-1_HIV-2: HIV-1 intergase antigen. The protein contains the HIV-1 immunodominant regions from pol protein (integrase). 1mg
00199-V Recombinant Viral Antigens HIV-1_HIV-2, HIV-1 intergase antigen. The protein contains the HIV-1 immunodominant regions from pol protein (integrase). 100ug/vial
EIAAB13421 Ecotropic viral integration site 5-like protein,EVI5L,EVI5-like protein,Homo sapiens,Human
00199-V Recombinant Viral antigens, HIV-1_HIV-2: HIV-1 intergase antigen. The protein contains the HIV-1 immunodominant regions from pol protein (integrase). 100ug/vial


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur