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

Sonic hedgehog protein A (SHHA) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) (VHH-1) [Cleaved into: Sonic hedgehog protein A N-product (Shh N-terminal processed signaling domains) (ShhNp) (Sonic hedgehog protein N-product) (ShhN)]

 SHH_DANRE               Reviewed;         418 AA.
Q92008; O13170; O13171; O13208; O13209; O13245; O13246;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=Sonic hedgehog protein A;
Short=SHHA;
AltName: Full=Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains {ECO:0000250|UniProtKB:Q62226};
Short=ShhNC {ECO:0000250|UniProtKB:Q62226};
AltName: Full=VHH-1;
Contains:
RecName: Full=Sonic hedgehog protein A N-product;
AltName: Full=Shh N-terminal processed signaling domains {ECO:0000250|UniProtKB:Q62226};
Short=ShhNp {ECO:0000250|UniProtKB:Q62226};
AltName: Full=Sonic hedgehog protein N-product;
Short=ShhN;
Flags: Precursor;
Name=shha; Synonyms=shh, vhh1;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=8124714; DOI=10.1016/0092-8674(94)90514-2;
Roelink H., Augsburger A., Heemskerk J., Korzh V., Norlin S.,
Ruiz i Altaba A., Tanabe Y., Placzek M., Edlund T., Jessell T.M.,
Dodd J.;
"Floor plate and motor neuron induction by vhh-1, a vertebrate homolog
of hedgehog expressed by the notochord.";
Cell 76:761-775(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC PROCESSING, AND AUTOCATALYTIC
CLEAVAGE.
PubMed=7583153; DOI=10.1016/S0960-9822(95)00185-0;
Ekker S.C., Ungar A.R., Greenstein P., von Kessler D.P., Porter J.A.,
Moon R.T., Beachy P.A.;
"Patterning activities of vertebrate hedgehog proteins in the
developing eye and brain.";
Curr. Biol. 5:944-955(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7579523;
Fietz M.J., Concordet J.-P., Barbosa R., Johnson R., Krauss S.,
McMahon A.P., Tabin C., Ingham P.W.;
"The hedgehog gene family in Drosophila and vertebrate development.";
Development Suppl. 120:43-51(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10207136;
Muller F., Chang B., Albert S., Fischer N., Tora L., Strahle U.;
"Intronic enhancers control expression of zebrafish sonic hedgehog in
floor plate and notochord.";
Development 126:2103-2116(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-92 AND 113-170.
TISSUE=Muscle;
PubMed=8917540; DOI=10.1073/pnas.93.23.13036;
Zardoya R., Abouheif E., Meyer A.;
"Evolutionary analyses of hedgehog and Hoxd-10 genes in fish species
closely related to the zebrafish.";
Proc. Natl. Acad. Sci. U.S.A. 93:13036-13041(1996).
-!- FUNCTION: Sonic hedgehog protein: The C-terminal part of the sonic
hedgehog protein precursor displays an autoproteolysis and a
cholesterol transferase activity (By similarity). Both activities
result in the cleavage of the full-length protein into two parts
(ShhN and ShhC) followed by the covalent attachment of a
cholesterol moiety to the C-terminal of the newly generated ShhN
(By similarity). Both activities occur in the reticulum
endoplasmic (By similarity). Once cleaved, ShhC is degraded in the
endoplasmic reticulum (By similarity).
{ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226,
ECO:0000269|PubMed:7583153}.
-!- FUNCTION: Sonic hedgehog protein N-product: The dually lipidated
sonic hedgehog protein N-product (ShhNp) is a morphogen which is
essential for a variety of patterning events during development.
Induces ventral cell fate in the neural tube and somites (By
similarity). Involved in the patterning of the anterior-posterior
axis of the developing limb bud (By similarity). Essential for
axon guidance (By similarity). Binds to the patched (PTCH1)
receptor, which functions in association with smoothened (SMO), to
activate the transcription of target genes (By similarity). In the
absence of SHH, PTCH1 represses the constitutive signaling
activity of SMO (By similarity). {ECO:0000250|UniProtKB:Q15465,
ECO:0000250|UniProtKB:Q62226}.
-!- SUBUNIT: Interacts with HHATL/GUP1 which negatively regulates
HHAT-mediated palmitoylation of the SHH N-terminus (By
similarity). ShhNp is active as a multimer (By similarity).
Interacts with BOC and CDON (By similarity). Interacts with HHIP
(By similarity). Interacts with DISP1 via its cholesterol anchor
(By similarity). Interacts with SCUBE2 (By similarity).
{ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226}.
-!- SUBCELLULAR LOCATION: Sonic hedgehog protein A N-product: Cell
membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor
{ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic
hedgehog protein N-product (ShhNp) is firmly tethered to the cell
membrane where it forms multimers (By similarity). Further
solubilization and release from the cell surface seem to be
achieved through different mechanisms, including the interaction
with DISP1 and SCUBE2, movement by lipoprotein particles,
transport by cellular extensions called cytonemes or by the
proteolytic removal of both terminal lipidated peptides.
{ECO:0000250|UniProtKB:Q62226}.
-!- TISSUE SPECIFICITY: Expressed in the ventral midline of the neural
tube and brain. Also found in the notochord and in developing fin
bud. In the developing brain, expression occurs in domains that
include a discrete region in the floor of the diencephalon.
-!- DEVELOPMENTAL STAGE: First detectable in the inner cell layer of
the embryonic shield during gastrulation. By 9.5 hours of
development, expressed in a continuous band that extends from the
tail to the head, the anterior boundary of expression being
positioned in the center of the animal pole anterior to the
presumptive midbrain.
-!- DOMAIN: Sonic hedgehog protein N-product: Binds calcium and zinc
ions; this stabilizes the protein fold and is essential for
protein-protein interactions mediated by this domain.
{ECO:0000250|UniProtKB:Q62226}.
-!- DOMAIN: Sonic hedgehog protein N-product: The Cardin-Weintraub
(CW) motif is required for heparan sulfate binding of the
solubilized ShhNp (By similarity). The N-terminal palmitoylated
peptide is cleaved at the Heparan sulfate-binding Cardin-Weintraub
(CW) motif site (By similarity). The cleavage reduced the
interactions with heparan sulfate. The cleavage is enhanced by
SCUBE2 (By similarity). {ECO:0000250|UniProtKB:Q62226}.
-!- PTM: The C-terminal domain displays an autoproteolysis activity
and a cholesterol transferase activity. Both activities result in
the cleavage of the full-length protein and covalent attachment of
a cholesterol moiety to the C-terminal of the newly generated N-
terminal fragment (N-product). The N-product is the active species
in both local and long-range signaling, whereas the C-product has
no signaling activity. {ECO:0000269|PubMed:7583153}.
-!- PTM: Sonic hedgehog protein: The C-terminal domain displays an
autoproteolysis activity and a cholesterol transferase activity
(By similarity). Both activities result in the cleavage of the
full-length protein and covalent attachment of a cholesterol
moiety to the C-terminal of the newly generated N-terminal
fragment (ShhN) (By similarity). Cholesterylation is required for
the sonic hedgehog protein N-product targeting to lipid rafts and
multimerization (By similarity). ShhN is the active species in
both local and long-range signaling, whereas the C-product (ShhC)
is degraded in the reticulum endoplasmic (By similarity).
{ECO:0000250|UniProtKB:Q62226, ECO:0000269|PubMed:7583153}.
-!- PTM: Sonic hedgehog protein N-product: N-palmitoylation by HHAT of
ShhN is required for sonic hedgehog protein N-product
multimerization and full activity (By similarity). It is a
prerequisite for the membrane-proximal positioning and the
subsequent shedding of this N-terminal peptide (By similarity).
{ECO:0000250|UniProtKB:Q62226}.
-!- PTM: Sonic hedgehog protein N-product: The lipidated N- and C-
terminal peptides of ShhNp can be cleaved (shedding) (By
similarity). The N-terminal palmitoylated peptide is cleaved at
the Cardin-Weintraub (CW) motif site (By similarity). The cleavage
reduced the interactions with heparan sulfate (By similarity). The
cleavage is enhanced by SCUBE2 (By similarity).
{ECO:0000250|UniProtKB:Q62226}.
-!- SIMILARITY: Belongs to the hedgehog family. {ECO:0000305}.
-!- CAUTION: The several steps and mechanisms that permit controlled
Shh dispersion and gradient formation remain controversial. The
ShhNC C-terminal domain displays an autoproteolysis activity and a
cholesterol transferase activity resulting in the cleavage and
covalent attachment of a cholesterol moiety to the C-terminal of
the newly generated N-terminal fragment (ShhN). The protein is
further modified by covalent addition of palmitate at the N-
terminal of ShhN, resulting to the dual-lipidated Shh (ShhNp).
ShhNp is firmly tethered to the cell membrane where it forms
multimers. Further solubilization and release from the cell
surface seem to be achieved through different mechanisms,
including the interaction with DISP1 and SCUBE2, movement by
lipoprotein particles, transport by cellular extensions called
cytonemes or by proteolytic removal of both terminal lipidated
peptides. Once released, the fully processed Shh can signal within
embryonic tissues both at short and long-range.
{ECO:0000250|UniProtKB:Q62226}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L27585; AAA20998.1; -; mRNA.
EMBL; U30711; AAC59742.1; -; mRNA.
EMBL; Z35669; CAA84738.1; -; mRNA.
EMBL; AF124382; AAD47913.1; -; Genomic_DNA.
EMBL; U51339; AAB38570.1; -; Genomic_DNA.
EMBL; U51351; AAB38575.1; -; Genomic_DNA.
EMBL; U51357; AAB38588.1; -; Genomic_DNA.
EMBL; U51370; AAB38593.1; -; Genomic_DNA.
PIR; A53193; A53193.
RefSeq; NP_571138.1; NM_131063.3.
UniGene; Dr.115833; -.
UniGene; Dr.36074; -.
ProteinModelPortal; Q92008; -.
SMR; Q92008; -.
STRING; 7955.ENSDARP00000125090; -.
MEROPS; C46.005; -.
PaxDb; Q92008; -.
Ensembl; ENSDART00000149395; ENSDARP00000125090; ENSDARG00000068567.
GeneID; 30269; -.
KEGG; dre:30269; -.
CTD; 30269; -.
ZFIN; ZDB-GENE-980526-166; shha.
eggNOG; KOG3638; Eukaryota.
eggNOG; ENOG410XQA3; LUCA.
GeneTree; ENSGT00390000001117; -.
HOVERGEN; HBG005480; -.
InParanoid; Q92008; -.
KO; K11988; -.
OMA; EHSWAHR; -.
OrthoDB; EOG091G0N90; -.
PhylomeDB; Q92008; -.
TreeFam; TF106458; -.
Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
Reactome; R-DRE-5362798; Release of Hh-Np from the secreting cell.
Reactome; R-DRE-5632681; Ligand-receptor interactions.
Reactome; R-DRE-5635838; Activation of SMO.
PRO; PR:Q92008; -.
Proteomes; UP000000437; Chromosome 7.
Bgee; ENSDARG00000068567; -.
ExpressionAtlas; Q92008; baseline.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:0021984; P:adenohypophysis development; IDA:ZFIN.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:ZFIN.
GO; GO:0007411; P:axon guidance; IMP:ZFIN.
GO; GO:0008015; P:blood circulation; IMP:ZFIN.
GO; GO:0007420; P:brain development; IMP:ZFIN.
GO; GO:0043010; P:camera-type eye development; IDA:ZFIN.
GO; GO:0010002; P:cardioblast differentiation; IMP:ZFIN.
GO; GO:0035143; P:caudal fin morphogenesis; IMP:ZFIN.
GO; GO:0001708; P:cell fate specification; IMP:ZFIN.
GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
GO; GO:0007368; P:determination of left/right symmetry; IDA:ZFIN.
GO; GO:0021536; P:diencephalon development; IGI:ZFIN.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
GO; GO:0031076; P:embryonic camera-type eye development; IMP:ZFIN.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:ZFIN.
GO; GO:0048702; P:embryonic neurocranium morphogenesis; IMP:ZFIN.
GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
GO; GO:0060956; P:endocardial cell differentiation; IGI:ZFIN.
GO; GO:0031018; P:endocrine pancreas development; IDA:ZFIN.
GO; GO:0042462; P:eye photoreceptor cell development; IMP:ZFIN.
GO; GO:0033504; P:floor plate development; IMP:ZFIN.
GO; GO:0021508; P:floor plate formation; IMP:ZFIN.
GO; GO:0030900; P:forebrain development; IMP:ZFIN.
GO; GO:0010001; P:glial cell differentiation; IMP:ZFIN.
GO; GO:0042063; P:gliogenesis; IMP:ZFIN.
GO; GO:0032835; P:glomerulus development; IMP:ZFIN.
GO; GO:0001947; P:heart looping; IDA:ZFIN.
GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
GO; GO:0048839; P:inner ear development; IGI:ZFIN.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
GO; GO:0030917; P:midbrain-hindbrain boundary development; IMP:ZFIN.
GO; GO:0042694; P:muscle cell fate specification; IMP:ZFIN.
GO; GO:0007517; P:muscle organ development; IMP:ZFIN.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:ZFIN.
GO; GO:0007399; P:nervous system development; IMP:ZFIN.
GO; GO:0001839; P:neural plate morphogenesis; IMP:ZFIN.
GO; GO:0030182; P:neuron differentiation; IMP:ZFIN.
GO; GO:0048663; P:neuron fate commitment; IGI:ZFIN.
GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
GO; GO:0048709; P:oligodendrocyte differentiation; IMP:ZFIN.
GO; GO:0070444; P:oligodendrocyte progenitor proliferation; IMP:ZFIN.
GO; GO:0031016; P:pancreas development; IDA:ZFIN.
GO; GO:0033339; P:pectoral fin development; IMP:ZFIN.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:ZFIN.
GO; GO:0048618; P:post-embryonic foregut morphogenesis; IMP:ZFIN.
GO; GO:0048793; P:pronephros development; IMP:ZFIN.
GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IDA:ZFIN.
GO; GO:0061035; P:regulation of cartilage development; IGI:ZFIN.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IMP:ZFIN.
GO; GO:0048741; P:skeletal muscle fiber development; IDA:ZFIN.
GO; GO:0007224; P:smoothened signaling pathway; IGI:ZFIN.
GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IMP:ZFIN.
GO; GO:0055002; P:striated muscle cell development; IMP:ZFIN.
GO; GO:0048795; P:swim bladder morphogenesis; IMP:ZFIN.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR001657; Hedgehog.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR000320; Hedgehog_signalling_dom.
InterPro; IPR001767; Hint_dom.
InterPro; IPR003586; Hint_dom_C.
InterPro; IPR003587; Hint_dom_N.
InterPro; IPR036844; Hint_dom_sf.
InterPro; IPR006141; Intein_N.
Pfam; PF01085; HH_signal; 1.
Pfam; PF01079; Hint; 1.
PIRSF; PIRSF009400; Peptidase_C46; 1.
PRINTS; PR00632; SONICHHOG.
SMART; SM00305; HintC; 1.
SMART; SM00306; HintN; 1.
SUPFAM; SSF51294; SSF51294; 1.
SUPFAM; SSF55166; SSF55166; 1.
PROSITE; PS50817; INTEIN_N_TER; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Calcium; Cell membrane; Complete proteome;
Developmental protein; Hydrolase; Lipoprotein; Membrane;
Metal-binding; Palmitate; Protease; Reference proteome; Signal; Zinc.
SIGNAL 1 23 {ECO:0000250|UniProtKB:Q15465}.
CHAIN 24 418 Sonic hedgehog protein A.
/FTId=PRO_0000013226.
CHAIN 24 197 Sonic hedgehog protein A N-product.
/FTId=PRO_0000013227.
MOTIF 32 38 Cardin-Weintraub.
{ECO:0000250|UniProtKB:Q62226}.
METAL 89 89 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 90 90 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 90 90 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 95 95 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 125 125 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q15465}.
METAL 126 126 Calcium 1.
{ECO:0000250|UniProtKB:Q15465}.
METAL 126 126 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 129 129 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 131 131 Calcium 2.
{ECO:0000250|UniProtKB:Q15465}.
METAL 140 140 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 147 147 Zinc. {ECO:0000250|UniProtKB:Q15465}.
METAL 182 182 Zinc. {ECO:0000250|UniProtKB:Q15465}.
SITE 197 198 Cleavage; by autolysis.
SITE 243 243 Involved in cholesterol transfer.
{ECO:0000250}.
SITE 267 267 Involved in auto-cleavage. {ECO:0000250}.
SITE 270 270 Essential for auto-cleavage.
{ECO:0000250}.
LIPID 24 24 N-palmitoyl cysteine. {ECO:0000250}.
LIPID 197 197 Cholesterol glycine ester. {ECO:0000250}.
SEQUENCE 418 AA; 46403 MW; CF000AFFFD2F5795 CRC64;
MRLLTRVLLV SLLTLSLVVS GLACGPGRGY GRRRHPKKLT PLAYKQFIPN VAEKTLGASG
RYEGKITRNS ERFKELTPNY NPDIIFKDEE NTGADRLMTQ RCKDKLNSLA ISVMNHWPGV
KLRVTEGWDE DGHHFEESLH YEGRAVDITT SDRDKSKYGT LSRLAVEAGF DWVYYESKAH
IHCSVKAENS VAAKSGGCFP GSALVSLQDG GQKAVKDLNP GDKVLAADSA GNLVFSDFIM
FTDRDSTTRR VFYVIETQEP VEKITLTAAH LLFVLDNSTE DLHTMTAAYA SSVRAGQKVM
VVDDSGQLKS VIVQRIYTEE QRGSFAPVTA HGTIVVDRIL ASCYAVIEDQ GLAHLAFAPA
RLYYYVSSFL FPQNSSSRSN ATLQQEGVHW YSRLLYQMGT WLLDSNMLHP LGMSVNSS


Related products :

Catalog number Product name Quantity
orb80579 Human Sonic HedgeHog His tag protein Sonic HedgeHog Recombinant Human produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids and having a molecular mass of 20.7k 5
orb80580 Mouse Sonic HedgeHog protein Sonic Hedgehog Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The 5
orb80100 Human Sonic HedgeHog protein Sonic HedgeHog Recombinant Human produced in E.coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19,683 Dalton 5
100-153 Sonic Hedgehog Human Host: E. coli Sonic Hedgehog 25
103-M269 Sonic Hedgehog (Shh) C-terminal Anti-Mouse Host: Rat Shh; Hx; Dsh; Hhg1; Hxl3; M100081; 9530036O11Rik 100
103-M269 Sonic Hedgehog (Shh) C-terminal, Host: Rat, Species: Anti-Mouse, Synonyms: Shh; Hx; Dsh; Hhg1; Hxl3; M100081; 9530036O11Rik 100 ug
18-272-196208 Sonic Hedgehog - Goat polyclonal to Sonic Hedgehog Polyclonal 0.05 mg
AJ1731a Sonic-Hedgehog (SHH) Antibody (C-Product)
ER601 Sonic hedgehog protein Elisa Kit 96T
CSB-EL021266RA Rat Sonic hedgehog protein(SHH) ELISA kit 96T
H2301 Sonic hedgehog protein (SHH), Rat, ELISA Kit 96T
EH605 Sonic hedgehog protein Elisa Kit 96T
orb90959 Human Sonic Hedgehog gene Human Sonic Hedgehog gene is a cDNA gene. For research use only. 10
14-8671-62 Mouse Sonic Hedgehog (SHH) Recombinant Protein 5 ug
H2299 Sonic hedgehog protein (SHH), Chicken, ELISA Kit 96T
orb80100 Human Sonic HedgeHog protein Proteins 5
H2300 Sonic hedgehog protein (SHH), Mouse, ELISA Kit 96T
CSB-EL021266CH Chicken Sonic hedgehog protein(SHH) ELISA kit 96T
CSB-EL021266MO Mouse Sonic hedgehog protein(SHH) ELISA kit 96T
CSB-EL021266RA Rat Sonic hedgehog protein(SHH) ELISA kit SpeciesRat 96T
orb80581 Mouse Sonic HedgeHog His tag protein Proteins 5
orb80580 Mouse Sonic HedgeHog protein Proteins 5
14-8679-80 Human Sonic Hedgehog (SHH) Recombinant Protein 25 ug
14-8679-62 Human Sonic Hedgehog (SHH) Recombinant Protein 5 ug
orb80579 Human Sonic HedgeHog His tag protein Proteins 5


 

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