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

Serine/arginine-rich splicing factor SR30 (At-SR30) (At-SRp30) (AtSR30) (SF2/ASF-like splicing modulator Srp30) (Serine-arginine rich RNA binding protein 30)

 SR30_ARATH              Reviewed;         268 AA.
Q9XFR5; Q949S8; Q9XFR6;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Serine/arginine-rich splicing factor SR30;
Short=At-SR30;
Short=At-SRp30;
Short=AtSR30;
AltName: Full=SF2/ASF-like splicing modulator Srp30;
AltName: Full=Serine-arginine rich RNA binding protein 30;
Name=SR30; Synonyms=SRP30; OrderedLocusNames=At1g09140;
ORFNames=T12M4.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
PubMed=10215626; DOI=10.1101/gad.13.8.987;
Lopato S., Kalyna M., Dorner S., Kobayashi R., Krainer A.R., Barta A.;
"atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana,
regulates splicing of specific plant genes.";
Genes Dev. 13:987-1001(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
INTERACTION WITH CYP63.
PubMed=15166240; DOI=10.1074/jbc.M400270200;
Lorkovic Z.J., Lopato S., Pexa M., Lehner R., Barta A.;
"Interactions of Arabidopsis RS domain containing cyclophilins with SR
proteins and U1 and U11 small nuclear ribonucleoprotein-specific
proteins suggest their involvement in pre-mRNA Splicing.";
J. Biol. Chem. 279:33890-33898(2004).
[6]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15034145; DOI=10.1091/mbc.E04-02-0100;
Fang Y., Hearn S., Spector D.L.;
"Tissue-specific expression and dynamic organization of SR splicing
factors in Arabidopsis.";
Mol. Biol. Cell 15:2664-2673(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=15133128; DOI=10.1091/mbc.E04-01-0055;
Lorkovic Z.J., Hilscher J., Barta A.;
"Use of fluorescent protein tags to study nuclear organization of the
spliceosomal machinery in transiently transformed living plant
cells.";
Mol. Biol. Cell 15:3233-3243(2004).
[8]
INTERACTION WITH SNRNP35.
PubMed=15987817; DOI=10.1261/rna.2440305;
Lorkovic Z.J., Lehner R., Forstner C., Barta A.;
"Evolutionary conservation of minor U12-type spliceosome between
plants and humans.";
RNA 11:1095-1107(2005).
[9]
INTERACTION WITH CYP59.
PubMed=16497658; DOI=10.1261/rna.2226106;
Gullerova M., Barta A., Lorkovic Z.J.;
"AtCyp59 is a multidomain cyclophilin from Arabidopsis thaliana that
interacts with SR proteins and the C-terminal domain of the RNA
polymerase II.";
RNA 12:631-643(2006).
[10]
ALTERNATIVE SPLICING, AND INDUCTION BY HIGH-LIGHT; PARAQUAT; COLD AND
SALT STRESS.
PubMed=17556373; DOI=10.1093/pcp/pcm069;
Tanabe N., Yoshimura K., Kimura A., Yabuta Y., Shigeoka S.;
"Differential expression of alternatively spliced mRNAs of Arabidopsis
SR protein homologs, atSR30 and atSR45a, in response to environmental
stress.";
Plant Cell Physiol. 48:1036-1049(2007).
[11]
ALTERNATIVE SPLICING, AND INDUCTION.
PubMed=17319848; DOI=10.1111/j.1365-313X.2006.03020.x;
Palusa S.G., Ali G.S., Reddy A.S.;
"Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich
proteins: regulation by hormones and stresses.";
Plant J. 49:1091-1107(2007).
[12]
ALTERNATIVE SPLICING.
PubMed=19734266; DOI=10.1104/pp.109.141705;
Chung T., Wang D., Kim C.S., Yadegari R., Larkins B.A.;
"Plant SMU-1 and SMU-2 homologues regulate pre-mRNA splicing and
multiple aspects of development.";
Plant Physiol. 151:1498-1512(2009).
[13]
GENE FAMILY, AND NOMENCLATURE.
PubMed=20884799; DOI=10.1105/tpc.110.078352;
Barta A., Kalyna M., Reddy A.S.;
"Implementing a rational and consistent nomenclature for
serine/arginine-rich protein splicing factors (SR proteins) in
plants.";
Plant Cell 22:2926-2929(2010).
[14]
GENE FAMILY.
PubMed=21935421; DOI=10.1371/journal.pone.0024542;
Richardson D.N., Rogers M.F., Labadorf A., Ben-Hur A., Guo H.,
Paterson A.H., Reddy A.S.N.;
"Comparative analysis of serine/arginine-rich proteins across 27
eukaryotes: insights into sub-family classification and extent of
alternative splicing.";
PLoS ONE 6:E24542-E24542(2011).
[15]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=23132568; DOI=10.1271/bbb.120425;
Mori T., Yoshimura K., Nosaka R., Sakuyama H., Koike Y., Tanabe N.,
Maruta T., Tamoi M., Shigeoka S.;
"Subcellular and subnuclear distribution of high-light responsive
serine/arginine-rich proteins, atSR45a and atSR30, in Arabidopsis
thaliana.";
Biosci. Biotechnol. Biochem. 76:2075-2081(2012).
[16]
INDUCTION.
PubMed=24763593; DOI=10.1126/science.1250322;
Petrillo E., Herz M.A., Fuchs A., Reifer D., Fuller J., Yanovsky M.J.,
Simpson C., Brown J.W., Barta A., Kalyna M., Kornblihtt A.R.;
"A chloroplast retrograde signal regulates nuclear alternative
splicing.";
Science 344:427-430(2014).
-!- FUNCTION: Regulatory splicing factor that modulates alternative
splicing and gene expression in specific cell types. Autoregulates
its own expression. Probably involved in intron recognition and
spliceosome assembly. {ECO:0000269|PubMed:10215626}.
-!- SUBUNIT: Component of the spliceosome. Interacts with SNRNP35,
CYP59 and CYP63. {ECO:0000269|PubMed:15166240,
ECO:0000269|PubMed:15987817, ECO:0000269|PubMed:16497658}.
-!- INTERACTION:
Q9LY75:CYP63; NbExp=4; IntAct=EBI-1540237, EBI-2360522;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15133128,
ECO:0000269|PubMed:23132568}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:15034145, ECO:0000269|PubMed:15133128,
ECO:0000269|PubMed:23132568}. Cytoplasm
{ECO:0000269|PubMed:23132568}. Note=Inhibition of phosphorylation
causes suppression of nuclear localization.
{ECO:0000269|PubMed:23132568}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9XFR5-1; Sequence=Displayed;
Name=2;
IsoId=Q9XFR5-2; Sequence=VSP_054988, VSP_054989;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10215626,
ECO:0000269|PubMed:15034145}.
-!- INDUCTION: Up-regulated by paraquat, high salt and early after
high-light irradiation. Down-regulated by cold.
{ECO:0000269|PubMed:17319848, ECO:0000269|PubMed:17556373,
ECO:0000269|PubMed:24763593}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:10215626,
ECO:0000269|PubMed:23132568}.
-!- MISCELLANEOUS: The splicing pattern of the pre-mRNA is regulated
in a tissue-specific manner and by development, and changes in
response to various types of stress treatment (PubMed:10215626,
PubMed:17556373, PubMed:17319848) or light regimes
(PubMed:24763593). {ECO:0000305|PubMed:10215626,
ECO:0000305|PubMed:17319848, ECO:0000305|PubMed:17556373,
ECO:0000305|PubMed:24763593}.
-!- MISCELLANEOUS: A mobile signal generated in the leaves triggers
root alternative splicing responses to light.
{ECO:0000305|PubMed:24763593}.
-!- SIMILARITY: Belongs to the splicing factor SR family. SR
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ131214; CAB42557.1; -; Genomic_DNA.
EMBL; AJ131214; CAB42558.1; -; Genomic_DNA.
EMBL; AC003114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002684; AEE28400.1; -; Genomic_DNA.
EMBL; CP002684; AEE28401.1; -; Genomic_DNA.
EMBL; AY150486; AAN13011.1; -; mRNA.
EMBL; AY050912; AAK93589.2; -; mRNA.
RefSeq; NP_172386.3; NM_100783.6. [Q9XFR5-1]
RefSeq; NP_683288.2; NM_148447.4. [Q9XFR5-2]
UniGene; At.419; -.
ProteinModelPortal; Q9XFR5; -.
SMR; Q9XFR5; -.
BioGrid; 22674; 11.
IntAct; Q9XFR5; 13.
STRING; 3702.AT1G09140.1; -.
iPTMnet; Q9XFR5; -.
PaxDb; Q9XFR5; -.
PRIDE; Q9XFR5; -.
EnsemblPlants; AT1G09140.1; AT1G09140.1; AT1G09140. [Q9XFR5-1]
EnsemblPlants; AT1G09140.2; AT1G09140.2; AT1G09140. [Q9XFR5-2]
EnsemblPlants; AT1G09140.3; AT1G09140.3; AT1G09140.
GeneID; 837433; -.
Gramene; AT1G09140.1; AT1G09140.1; AT1G09140.
Gramene; AT1G09140.2; AT1G09140.2; AT1G09140.
Gramene; AT1G09140.3; AT1G09140.3; AT1G09140.
KEGG; ath:AT1G09140; -.
Araport; AT1G09140; -.
TAIR; locus:2195346; AT1G09140.
eggNOG; KOG0105; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000276234; -.
InParanoid; Q9XFR5; -.
KO; K12890; -.
OMA; GEVSYIR; -.
OrthoDB; EOG09360OW1; -.
PhylomeDB; Q9XFR5; -.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-72165; mRNA Splicing - Minor Pathway.
PRO; PR:Q9XFR5; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9XFR5; baseline and differential.
Genevisible; Q9XFR5; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0035061; C:interchromatin granule; IDA:TAIR.
GO; GO:0016607; C:nuclear speck; IDA:TAIR.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; ISS:TAIR.
GO; GO:0006376; P:mRNA splice site selection; IMP:TAIR.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:TAIR.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Spliceosome.
CHAIN 1 268 Serine/arginine-rich splicing factor
SR30.
/FTId=PRO_0000429595.
DOMAIN 7 82 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 109 187 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 181 267 Arg/Ser-rich (RS domain).
MOD_RES 193 193 Phosphoserine.
{ECO:0000250|UniProtKB:P92964}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000250|UniProtKB:P92965}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VYA5}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VYA5}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:P92964}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:Q9FYB7}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:P92966}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q9SJA6}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:P92965}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q9FYB7}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000250|UniProtKB:P92966}.
VAR_SEQ 247 256 QSRSKSRSRS -> GSLLRAGDWI (in isoform 2).
{ECO:0000303|PubMed:10215626}.
/FTId=VSP_054988.
VAR_SEQ 257 268 Missing (in isoform 2).
{ECO:0000303|PubMed:10215626}.
/FTId=VSP_054989.
CONFLICT 110 110 R -> H (in Ref. 4; AAK93589).
{ECO:0000305}.
CONFLICT 254 254 S -> T (in Ref. 4; AAK93589).
{ECO:0000305}.
SEQUENCE 268 AA; 30386 MW; 73BDC3534A8F9AC4 CRC64;
MSSRWNRTIY VGNLPGDIRK CEVEDLFYKY GPIVDIDLKI PPRPPGYAFV EFEDPRDADD
AIYGRDGYDF DGCRLRVEIA HGGRRFSPSV DRYSSSYSAS RAPSRRSDYR VLVTGLPPSA
SWQDLKDHMR KAGDVCFSEV FPDRKGMSGV VDYSNYDDMK YAIRKLDATE FRNAFSSAYI
RVREYESRSV SRSPDDSKSY RSRSRSRGPS CSYSSKSRSV SPARSISPRS RPLSRSRSLY
SSVSRSQSRS KSRSRSRSNS PVSPVISG


Related products :

Catalog number Product name Quantity
EIAAB39954 40 kDa SR-repressor protein,FUS-interacting serine-arginine-rich protein 1,FUSIP1,FUSIP2,Homo sapiens,Human,Serine_arginine-rich splicing factor 10,SFRS13A,Splicing factor SRp38,Splicing factor, argin
EIAAB38025 Homo sapiens,Human,SCAF,SCAF1,Serine arginine-rich pre-mRNA splicing factor SR-A1,SFRS19,Splicing factor, arginine_serine-rich 19,SRA1,SR-A1,SR-related and CTD-associated factor 1,SR-related-CTD-assoc
PR-774 ASF per SF2 (SFRS1 or SRp30a)His Splicing Factor, Arginine per Serine-rich 1, Pre-mRNA Splicing Factor human, recombinant, E. coli 10
PR-775 ASF per SF2 (SFRS1 or SRp30a)His Splicing Factor, Arginine per Serine-rich 1, Pre-mRNA Splicing Factor human, recombinant, Sf9 insect cells 5
EIAAB39955 Arginine-rich 54 kDa nuclear protein,Homo sapiens,Human,p54,Serine_arginine-rich splicing factor 11,SFRS11,Splicing factor, arginine_serine-rich 11,SRSF11
EH1319 Serine per arginine-rich splicing factor 3 Elisa Kit 96T
EH1318 Serine per arginine-rich splicing factor 2 Elisa Kit 96T
E1850h Rat ELISA Kit FOR Serine per arginine-rich splicing factor 5 96T
EH2379 Serine per arginine-rich splicing factor 1 Elisa Kit 96T
RPR-352 Recombinant Human Serine arginine-Rich Splicing Factor 1 5
E0014Rb Rabbit ELISA Kit FOR Serine per arginine-rich splicing factor 6 96T
OS9_BOVIN Human ELISA Kit FOR Serine per arginine-rich splicing factor 9 96T
K1737_HUMAN Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
CNTLN_HUMAN Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 12 96T
H2879 Splicing factor, arginine serine-rich 19 (SCAF1), Rat, ELISA Kit 96T
BLCAP_BOVIN Rabbit ELISA Kit FOR Serine per arginine-rich splicing factor 6 96T
RPP14_MOUSE Rabbit ELISA Kit FOR Serine per arginine-rich splicing factor 6 96T
PP1G_BOVIN Human ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
E0056c Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 12 96T
E1213r Human ELISA Kit FOR Serine per arginine-rich splicing factor 8 96T
pro-1352 Recombinant Human Serine per arginine-Rich Splicing Factor 1 20
E0485h Human ELISA Kit FOR Serine per arginine-rich splicing factor 9 96T
ARNT2_RAT Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
E0321c Mouse ELISA Kit FOR Serine per arginine-rich splicing factor 4 96T
pro-1352 Recombinant Human Serine per arginine-Rich Splicing Factor 1 1mg


 

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