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

Capsid scaffolding protein (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease); Assembly protein (Capsid assembly protein)]

 T2FL05_9ALPH            Unreviewed;       532 AA.
T2FL05;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
27-SEP-2017, entry version 20.
RecName: Full=Capsid scaffolding protein {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Protease precursor {ECO:0000256|HAMAP-Rule:MF_04008};
Short=pPR {ECO:0000256|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Capsid assembly protein {ECO:0000256|HAMAP-Rule:MF_04008};
Contains:
RecName: Full=Assemblin {ECO:0000256|HAMAP-Rule:MF_04008};
EC=3.4.21.97 {ECO:0000256|HAMAP-Rule:MF_04008};
AltName: Full=Protease {ECO:0000256|HAMAP-Rule:MF_04008};
Name=UL26 {ECO:0000313|EMBL:AGW01120.1};
Suid alphaherpesvirus 1 (Pseudorabies virus).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Varicellovirus.
NCBI_TaxID=10345 {ECO:0000313|EMBL:AGW01120.1, ECO:0000313|Proteomes:UP000166532};
[1] {ECO:0000313|EMBL:AGW01120.1, ECO:0000313|Proteomes:UP000166532}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BJ/YT {ECO:0000313|EMBL:AGW01120.1};
Zhong C., Lyu Y.L., Liu L., Zhang L.T., Lu Z.J., Wang J.S.;
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AIT55771.1, ECO:0000313|Proteomes:UP000142350}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TJ {ECO:0000313|EMBL:AIT55771.1};
PubMed=25293398; DOI=10.1016/j.vetmic.2014.09.003;
Luo Y., Li N., Cong X., Wang C.H., Du M., Li L., Zhao B., Yuan J.,
Liu D.D., Li S., Li Y., Sun Y., Qiu H.J.;
"Pathogenicity and genomic characterization of a pseudorabies virus
variant isolated from Bartha-K61-vaccinated swine population in
China.";
Vet. Microbiol. 174:107-115(2014).
[3] {ECO:0000313|EMBL:AJD79513.1, ECO:0000313|Proteomes:UP000119561}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ZJ01 {ECO:0000313|EMBL:AJD79513.1};
Gu Z., Dong J., Sun H., Yang W., Hou C., Bai J., Jiang P.;
"Comparetive analysis of the highly pathogenic variant of pseudorabies
virus strain ZJ01.";
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:AKG93996.1}
NUCLEOTIDE SEQUENCE.
STRAIN=HNX {ECO:0000313|EMBL:AKG93996.1};
Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:AKG93996.1, ECO:0000313|Proteomes:UP000144334}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HNX {ECO:0000313|EMBL:AKG93996.1};
PubMed=26370151; DOI=10.1021/acsami.5b06876;
Ye S., Shao K., Li Z., Guo N., Zuo Y., Li Q., Lu Z., Chen L., He Q.,
Han H.;
"Antiviral Activity of Graphene Oxide: How Sharp Edged Structure and
Charge Matter.";
ACS Appl Mater Interfaces 7:21571-21579(2015).
[6] {ECO:0000313|EMBL:AJW72265.1, ECO:0000313|Proteomes:UP000113972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HeN1 {ECO:0000313|EMBL:AJW72265.1};
PubMed=25965793; DOI=10.1016/j.virol.2015.04.013;
Ye C., Zhang Q.Z., Tian Z.J., Zheng H., Zhao K., Liu F., Guo J.C.,
Tong W., Jiang C.G., Wang S.J., Shi M., Chang X.B., Jiang Y.F.,
Peng J.M., Zhou Y.J., Tang Y.D., Sun M.X., Cai X.H., An T.Q.,
Tong G.Z.;
"Genomic characterization of emergent pseudorabies virus in China
reveals marked sequence divergence: Evidence for the existence of two
major genotypes.";
Virology 483:32-43(2015).
[7] {ECO:0000313|EMBL:ALT14251.1}
NUCLEOTIDE SEQUENCE.
STRAIN=HN1201 {ECO:0000313|EMBL:ALT14251.1};
Xiang T., Song Y., Huang L., Wang B., Wu P.;
Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:ANR01145.1}
NUCLEOTIDE SEQUENCE.
STRAIN=HB1201 {ECO:0000313|EMBL:ANR01145.1};
Ge X., Li M., Zhou L., Guo X., Yang H.;
"The recently emergent PRV strain isolated from a Bartha-K61-
vaccinated piglet in China.";
Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:ANZ03059.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Ea {ECO:0000313|EMBL:ANZ03059.1};
Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AKG94128.1, ECO:0000313|Proteomes:UP000150587}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HNB {ECO:0000313|EMBL:AKG94128.1};
PubMed=26823587;
Yu T., Chen F., Ku X., Zhu Y., Ma H., Li S., He Q.;
"Complete Genome Sequence of Novel Pseudorabies Virus Strain HNB
Isolated in China.";
Genome Announc. 4:e01641-15(2016).
[11] {ECO:0000313|EMBL:ALT14251.1, ECO:0000313|Proteomes:UP000154438}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HN1201 {ECO:0000313|EMBL:ALT14251.1};
PubMed=26988055;
Xiang S., Zhou Z., Hu X., Li Y., Zhang C., Wang J., Li X., Tan F.,
Tian K.;
"Complete Genome Sequence of a Variant Pseudorabies Virus Strain
Isolated in Central China.";
Genome Announc. 4:0-0(2016).
[12] {ECO:0000313|EMBL:AML81212.1, ECO:0000313|Proteomes:UP000104419}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HLJ8 {ECO:0000313|EMBL:AML81212.1};
PubMed=26874017; DOI=10.1016/j.virol.2016.01.016;
Ye C., Guo J.C., Gao J.C., Wang T.Y., Zhao K., Chang X.B., Wang Q.,
Peng J.M., Tian Z.J., Cai X.H., Tong G.Z., An T.Q.;
"Genomic analyses reveal that partial sequence of an earlier
pseudorabies virus in China is originated from a Bartha-vaccine-like
strain.";
Virology 491:56-63(2016).
[13] {ECO:0000313|EMBL:AKG94062.1, ECO:0000313|Proteomes:UP000128799}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Fa {ECO:0000313|EMBL:AKG94062.1};
PubMed=27012685; DOI=10.1007/s11262-016-1324-z;
Yu T., Chen F., Ku X., Fan J., Zhu Y., Ma H., Li S., Wu B., He Q.;
"Growth characteristics and complete genomic sequence analysis of a
novel pseudorabies virus in China.";
Virus Genes 52:474-483(2016).
[14] {ECO:0000313|EMBL:ARJ55461.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Ea {ECO:0000313|EMBL:ARJ55461.1};
PubMed=28363130; DOI=.1016/j.virol.2017.03.013;
Wang X., Wu C.X., Song X.R., Chen H.C., Liu Z.F.;
"Comparison of pseudorabies virus China reference strain with emerging
variants reveals independent virus evolution within specific
geographic regions.";
Virology 506:92-98(2017).
-!- FUNCTION: Assemblin: Protease that plays an essential role in
virion assembly within the nucleus. Catalyzes the cleavage of the
assembly protein after formation of the spherical procapsid. By
that cleavage, the capsid matures and gains its icosahedral shape.
The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well
as Ala-Thr bonds. Assemblin and cleavages products are evicted
from the capsid before or during DNA packaging.
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- FUNCTION: Assembly protein: Plays a major role in capsid assembly.
Acts as a scaffold protein by binding major capsid protein.
Multimerizes in the nucleus such as major capsid protein forms the
icosahedral T=16 capsid. Cleaved by assemblin after capsid
completion. The cleavages products are evicted from the capsid
before or during DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- FUNCTION: Capsid scaffolding protein: Acts as a scaffold protein
by binding major capsid protein in the cytoplasm, inducing the
nuclear localization of both proteins. Multimerizes in the nucleus
such as major capsid protein forms the icosahedral T=16 capsid.
Autocatalytic cleavage releases the assembly protein, and
subsequently abolishes interaction with major capsid protein.
Cleavages products are evicted from the capsid before or during
DNA packaging. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- CATALYTIC ACTIVITY: Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in
the scaffold protein. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- SUBUNIT: Capsid scaffolding protein homomultimerizes and interacts
with major capsid protein. Assemblin exists in a monomer-dimer
equilibrium with the dimer being the active species. Assembly
protein homomultimerizes and interacts with major capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- DOMAIN: Region of interaction between pPR and pAP is called Amino
conserved domain (ACD). The region of interaction with major
capsid protein is called carboxyl conserved domain (CCD).
{ECO:0000256|HAMAP-Rule:MF_04008}.
-!- PTM: Capsid scaffolding protein is cleaved by assemblin after
formation of the spherical procapsid. As a result, the capsid
obtains its mature, icosahedral shape. Cleavages occur at two or
more sites: release and tail site. {ECO:0000256|HAMAP-
Rule:MF_04008}.
-!- SIMILARITY: Belongs to the herpesviridae capsid scaffolding
protein family. {ECO:0000256|HAMAP-Rule:MF_04008}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04008}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; KC981239; AGW01120.1; -; Genomic_DNA.
EMBL; KJ789182; AIT55771.1; -; Genomic_DNA.
EMBL; KM061380; AJD79513.1; -; Genomic_DNA.
EMBL; KP098534; AJW72265.1; -; Genomic_DNA.
EMBL; KM189912; AKG93996.1; -; Genomic_DNA.
EMBL; KM189913; AKG94062.1; -; Genomic_DNA.
EMBL; KM189914; AKG94128.1; -; Genomic_DNA.
EMBL; KP722022; ALT14251.1; -; Genomic_DNA.
EMBL; KT824771; AML81212.1; -; Genomic_DNA.
EMBL; KU057086; ANR01145.1; -; Genomic_DNA.
EMBL; KU315430; ANZ03059.1; -; Genomic_DNA.
EMBL; KX423960; ARJ55461.1; -; Genomic_DNA.
Proteomes; UP000104419; Genome.
Proteomes; UP000113972; Genome.
Proteomes; UP000119561; Genome.
Proteomes; UP000128799; Genome.
Proteomes; UP000142350; Genome.
Proteomes; UP000144334; Genome.
Proteomes; UP000150587; Genome.
Proteomes; UP000154438; Genome.
Proteomes; UP000166532; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
Gene3D; 3.20.16.10; -; 1.
HAMAP; MF_04008; HSV_SCAF; 1.
InterPro; IPR035443; Herpes_virus/Caudovirus_domain.
InterPro; IPR001847; Peptidase_S21.
Pfam; PF00716; Peptidase_S21; 1.
PRINTS; PR00236; HSVCAPSIDP40.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000104419,
ECO:0000313|Proteomes:UP000113972, ECO:0000313|Proteomes:UP000119561,
ECO:0000313|Proteomes:UP000128799};
Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04008};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04008};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04008};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04008};
Protease {ECO:0000256|HAMAP-Rule:MF_04008};
Serine protease {ECO:0000256|HAMAP-Rule:MF_04008};
Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04008};
Virus exit from host cell {ECO:0000256|HAMAP-Rule:MF_04008}.
REGION 512 532 Interaction with major capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04008}.
ACT_SITE 43 43 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
ACT_SITE 109 109 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
ACT_SITE 128 128 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_04008}.
SITE 225 226 Cleavage; by assemblin; Release site.
{ECO:0000256|HAMAP-Rule:MF_04008}.
SEQUENCE 532 AA; 55456 MW; AD95B81B08FACAB5 CRC64;
MGPVYVSGYL ALYDRDGGEL ALTREVVAAA LPPAGPLPIN IDHRPRCDIG AVLAVVDDDR
GPFFLGVVNC PQLGAVLARA VGPDFFGDMR LSDEERLLYL LSNYLPSASL SSRRLAPGEA
PDETLFAHVA LCVIGRRVGT IVVYDASPEA AVAPFRQLSA RARSELLARA AESPDRERVW
HMSEEALTRA LLSTAVNNML LRDRWELVAA RRREAGVRGH TYLQATMWAG LLPKSGASPA
PGPSAAMAAP PSAAPGDYIF VPAAQYNQLV VNQRPAPSLE SQLGAIVSAA MDRRHRRSPS
PEPRPPARKR RYDDYAQDNA YYPGEAPPPA SDLAAVVSSL QREISHLRAQ QLRYPTPYYA
PATPPQLLPP GLPPGAVVGH AHQHPHHAAG ALYPPMYAHQ PGLHAPPPSP VAHAVPALPG
LPGLQGLAAP VAHVPAQVVP QQPVVVQAQP VAVPAAAAAA AAPAPAPAAA AAAAAPVQAA
APAAPASAPQ PPVQASVSAP ADVSAGTIDA SSAAVACQRG ADIFVSQMMS HR


Related products :

Catalog number Product name Quantity
65-004 anti_HIV_1 Gag p24 antibody, rabbit serum HIV_1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. T 50 ul
65-005 anti_HIV_1 Gag p24 antibody, rabbit serum HIV_1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. T 250 ul
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
SCH-OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
orb81775 Rubella Virus Capsid C protein The E.coli derived recombinant protein contains the Rubella Virus Capsid regions, 1-123 amino acids. For research use only. 100
18-272-195346 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.05 ml
18-272-197033 Amyloid Precursor Protein - Goat polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 P 0.05 ml
18-272-197032 Amyloid Precursor Protein - Goat polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 P 0.05 ml
18-272-195345 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.05 ml
18-272-196327 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.5 ml
18-272-197027 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.1 mg
18-272-197028 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.1 mg
20-272-190769 Amyloid Precursor Protein - Mouse monoclonal [3E9] to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; 0.05 mg
MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
SCH-MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
18-272-196328 Amyloid Precursor Protein prediluted - Rabbit polyclonal to Amyloid Precursor Protein prediluted; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin- 7 ml
orb70744 CMV Assemblin Protease Substrate (M-site) peptide This is CMV Assemblin Protease Substrate (M-site) peptide. For research use only. 1 mg
EIAAB44303 Cancer_testis antigen 20,CT20,Homo sapiens,Human,Probable threonine protease PRSS50,PRSS50,Serine protease 50,Testis-specific protease-like protein 50,TSP50
orb82441 Rubella Virus Capsid, recombinant protein Rubella Capsid (C), Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
orb80921 Human Assembly Protein Complex 2 protein Assembly Protein Complex Human Recombinant produced in E.coli is non-glycosylated, polypeptide chain containing amino acids (1-435) and having total molecular 2
orb80922 Human Assembly Protein Complex 3 protein Assembly Protein Complex Human Recombinant produced in E.coli is non-glycosylated, polypeptide chain containing amino acids (1-193) and having total molecular 2
EIAAB42587 Airway trypsin-like protease 1,ECRG1,Epidermal type-II transmembrane serine protease,Esophageal cancer-susceptibility gene 1 protein,HATL1,HESP,Homo sapiens,Human,TMPRSS11A,Transmembrane protease seri


 

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