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

Protein S100-A8 (Calgranulin-A) (Chemotactic cytokine CP-10) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (Pro-inflammatory S100 cytokine) (S100 calcium-binding protein A8)

 S10A8_MOUSE             Reviewed;          89 AA.
P27005; P31724;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 147.
RecName: Full=Protein S100-A8;
AltName: Full=Calgranulin-A;
AltName: Full=Chemotactic cytokine CP-10;
AltName: Full=Leukocyte L1 complex light chain;
AltName: Full=Migration inhibitory factor-related protein 8;
Short=MRP-8;
Short=p8;
AltName: Full=Pro-inflammatory S100 cytokine;
AltName: Full=S100 calcium-binding protein A8;
Name=S100a8; Synonyms=Caga, Mrp8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1373330;
Lagasse E., Weissman I.L.;
"Mouse MRP8 and MRP14, two intracellular calcium-binding proteins
associated with the development of the myeloid lineage.";
Blood 79:1907-1915(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8454868;
Lackmann M., Rajasekariah P., Iismaa S.E., Jones G., Cornish C.J.,
Hu S., Simpson R.J., Moritz R.L., Geczy C.L.;
"Identification of a chemotactic domain of the pro-inflammatory S100
protein CP-10.";
J. Immunol. 150:2981-2991(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ; TISSUE=Liver;
PubMed=8611640; DOI=10.1016/0925-4439(95)00108-5;
Nacken W.K.F., Manitz M.P., Sorg C.;
"Molecular characterisation of the genomic locus of the mouse MRP8
gene.";
Biochim. Biophys. Acta 1315:1-5(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-77.
TISSUE=Spleen;
PubMed=1559987;
Lackmann M., Cornish C.J., Simpson R.J., Moritz R.L., Geczy C.L.;
"Purification and structural analysis of a murine chemotactic cytokine
(CP-10) with sequence homology to S100 proteins.";
J. Biol. Chem. 267:7499-7504(1992).
[6]
DISRUPTION PHENOTYPE.
PubMed=10438963;
Passey R.J., Williams E., Lichanska A.M., Wells C., Hu S., Geczy C.L.,
Little M.H., Hume D.A.;
"A null mutation in the inflammation-associated S100 protein S100A8
causes early resorption of the mouse embryo.";
J. Immunol. 163:2209-2216(1999).
[7]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH TLR4 AND
LY96.
PubMed=17767165; DOI=10.1038/nm1638;
Vogl T., Tenbrock K., Ludwig S., Leukert N., Ehrhardt C.,
van Zoelen M.A.D., Nacken W., Foell D., van der Poll T., Sorg C.,
Roth J.;
"Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4,
promoting lethal, endotoxin-induced shock.";
Nat. Med. 13:1042-1049(2007).
[8]
FUNCTION, AND INTERACTION WITH AGER AND ATP2A2.
PubMed=18403730; DOI=10.1161/CIRCRESAHA.107.167544;
Boyd J.H., Kan B., Roberts H., Wang Y., Walley K.R.;
"S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction
via the receptor for advanced glycation end products.";
Circ. Res. 102:1239-1246(2008).
[9]
S-NITROSYLATION AT CYS-42.
PubMed=18832721; DOI=10.4049/jimmunol.181.8.5627;
Lim S.Y., Raftery M., Cai H., Hsu K., Yan W.X., Hseih H.L.,
Watts R.N., Richardson D., Thomas S., Perry M., Geczy C.L.;
"S-nitrosylated S100A8: novel anti-inflammatory properties.";
J. Immunol. 181:5627-5636(2008).
[10]
REVIEW.
PubMed=20523765; DOI=10.2174/187152309789838975;
Hsu K., Champaiboon C., Guenther B.D., Sorenson B.S., Khammanivong A.,
Ross K.F., Geczy C.L., Herzberg M.C.;
"Anti-infective protective properties of S100 calgranulins.";
Antiinflamm. Antiallergy Agents Med. Chem. 8:290-305(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
REVIEW.
PubMed=20213444; DOI=10.1007/s00726-010-0528-0;
Goyette J., Geczy C.L.;
"Inflammation-associated S100 proteins: new mechanisms that regulate
function.";
Amino Acids 41:821-842(2011).
-!- FUNCTION: S100A8 is a calcium- and zinc-binding protein which
plays a prominent role in the regulation of inflammatory processes
and immune response. It can induce neutrophil chemotaxis and
adhesion. Predominantly found as calprotectin (S100A8/A9) which
has a wide plethora of intra- and extracellular functions. The
intracellular functions include: facilitating leukocyte
arachidonic acid trafficking and metabolism, modulation of the
tubulin-dependent cytoskeleton during migration of phagocytes and
activation of the neutrophilic NADPH-oxidase. Activates NADPH-
oxidase by facilitating the enzyme complex assembly at the cell
membrane, transferring arachidonic acid, an essential cofactor, to
the enzyme complex and S100A8 contributes to the enzyme assembly
by directly binding to NCF2/P67PHOX. The extracellular functions
involve proinflammatory, antimicrobial, oxidant-scavenging and
apoptosis-inducing activities. Its proinflammatory activity
includes recruitment of leukocytes, promotion of cytokine and
chemokine production, and regulation of leukocyte adhesion and
migration. Acts as an alarmin or a danger associated molecular
pattern (DAMP) molecule and stimulates innate immune cells via
binding to pattern recognition receptors such as Toll-like
receptor 4 (TLR4) and receptor for advanced glycation endproducts
(AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-
kappa-B signaling pathways resulting in the amplification of the
proinflammatory cascade. Has antimicrobial activity towards
bacteria and fungi and exerts its antimicrobial activity probably
via chelation of Zn(2+) which is essential for microbial growth.
Can induce cell death via autophagy and apoptosis and this occurs
through the cross-talk of mitochondria and lysosomes via reactive
oxygen species (ROS) and the process involves BNIP3. Can regulate
neutrophil number and apoptosis by an anti-apoptotic effect;
regulates cell survival via ITGAM/ITGB and TLR4 and a signaling
mechanism involving MEK-ERK. Its role as an oxidant scavenger has
a protective role in preventing exaggerated tissue damage by
scavenging oxidants. The iNOS-S100A8/A9 transnitrosylase complex
is proposed to direct selective inflammatory stimulus-dependent S-
nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN
and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to
contribute to S-nitrosylation site selectivity (By similarity).
{ECO:0000250|UniProtKB:P05109, ECO:0000269|PubMed:17767165,
ECO:0000269|PubMed:18403730}.
-!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
heterotetramer with S100A9 known as calprotectin (S100A8/A9).
Calprotectin (S100A8/9) interacts with CEACAM3 and tubulin
filaments in a calcium-dependent manner. Heterotetrameric
calprotectin (S100A8/A9) interacts with ANXA6 and associates with
tubulin filaments in activated monocytes. S100A8 and calprotectin
(S100A8/9) interact with NCF2/P67PHOX, RAC1 and RAC2. Calprotectin
(S100A8/9) interacts with CYBA and CYBB (By similarity). S100A8
interacts with AGER, ATP2A2 and with the heterodimeric complex
formed by TLR4 and LY96. Calprotectin (S100A8/9) interacts with
NOS2 to form the iNOS-S100A8/A9 transnitrosylase complex (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05109,
ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17767165}.
Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Cell membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=Predominantly localized in the cytoplasm. Upon
elevation of the intracellular calcium level, translocated from
the cytoplasm to the cytoskeleton and the cell membrane. Upon
neutrophil activation or endothelial adhesion of monocytes, is
secreted via a microtubule-mediated, alternative pathway.
-!- DISRUPTION PHENOTYPE: Death at an early embryonic stage due to
embryo resorption, starting about 8 days after fertilization.
{ECO:0000269|PubMed:10438963}.
-!- MISCELLANEOUS: Binds two calcium ions per molecule with an
affinity similar to that of the S-100 proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M83218; AAB07229.1; -; mRNA.
EMBL; S57123; AAB25840.1; -; mRNA.
EMBL; X87966; CAA61204.1; -; Genomic_DNA.
EMBL; BC078629; AAH78629.1; -; mRNA.
CCDS; CCDS38507.1; -.
PIR; I56163; I56163.
RefSeq; NP_038678.1; NM_013650.2.
UniGene; Mm.21567; -.
ProteinModelPortal; P27005; -.
SMR; P27005; -.
ComplexPortal; CPX-40; Calprotectin heterotetramer.
ComplexPortal; CPX-41; Calprotectin heterodimer.
ComplexPortal; CPX-47; S100A8 complex.
ComplexPortal; CPX-53; iNOS-S100A8/A9 complex.
IntAct; P27005; 3.
MINT; P27005; -.
STRING; 10090.ENSMUSP00000064385; -.
iPTMnet; P27005; -.
PhosphoSitePlus; P27005; -.
PaxDb; P27005; -.
PeptideAtlas; P27005; -.
PRIDE; P27005; -.
Ensembl; ENSMUST00000069927; ENSMUSP00000064385; ENSMUSG00000056054.
GeneID; 20201; -.
KEGG; mmu:20201; -.
UCSC; uc008qdd.1; mouse.
CTD; 6279; -.
MGI; MGI:88244; S100a8.
eggNOG; ENOG410J2UM; Eukaryota.
eggNOG; ENOG4111CN5; LUCA.
GeneTree; ENSGT00910000144329; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P27005; -.
KO; K21127; -.
OMA; IKGNYHA; -.
OrthoDB; EOG091G13NB; -.
PhylomeDB; P27005; -.
TreeFam; TF332727; -.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
PRO; PR:P27005; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000056054; Expressed in 166 organ(s), highest expression level in bone marrow.
CleanEx; MM_S100A8; -.
ExpressionAtlas; P27005; baseline and differential.
Genevisible; P27005; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0050544; F:arachidonic acid binding; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0050786; F:RAGE receptor binding; IEA:InterPro.
GO; GO:0035662; F:Toll-like receptor 4 binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0014002; P:astrocyte development; IGI:MGI.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISO:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0002793; P:positive regulation of peptide secretion; IDA:MGI.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028474; S100A8.
PANTHER; PTHR11639:SF5; PTHR11639:SF5; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
Antimicrobial; Antioxidant; Apoptosis; Autophagy; Calcium;
Cell membrane; Chemotaxis; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Immunity; Inflammatory response;
Innate immunity; Membrane; Metal-binding; Reference proteome; Repeat;
S-nitrosylation; Secreted; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1559987}.
CHAIN 2 89 Protein S100-A8.
/FTId=PRO_0000143994.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 46 81 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 20 33 1; low affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 59 70 2; high affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
METAL 17 17 Zinc. {ECO:0000250}.
METAL 27 27 Zinc. {ECO:0000250}.
METAL 83 83 Zinc. {ECO:0000250}.
MOD_RES 42 42 S-nitrosocysteine.
{ECO:0000269|PubMed:18832721}.
CONFLICT 57 57 E -> D (in Ref. 3; CAA61204).
{ECO:0000305}.
SEQUENCE 89 AA; 10295 MW; D2AFF46ACE867A28 CRC64;
MPSELEKALS NLIDVYHNYS NIQGNHHALY KNDFKKMVTT ECPQFVQNIN IENLFRELDI
NSDNAINFEE FLAMVIKVGV ASHKDSHKE


Related products :

Catalog number Product name Quantity
U1792m CLIA kit Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine,P 96T
E1792m ELISA kit Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine, 96T
E1792m ELISA Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine,Prote 96T
U1792m CLIA Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine,Protei 96T
E1793m ELISA Cagb,Calgranulin-B,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,Mouse,Mrp14,MRP-14,Mus musculus,p14,Protein S100-A9,S100 calcium-binding protein A9,S100a9 96T
U1793m CLIA Cagb,Calgranulin-B,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,Mouse,Mrp14,MRP-14,Mus musculus,p14,Protein S100-A9,S100 calcium-binding protein A9,S100a9 96T
E1793m ELISA kit Cagb,Calgranulin-B,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,Mouse,Mrp14,MRP-14,Mus musculus,p14,Protein S100-A9,S100 calcium-binding protein A9,S100a9 96T
U1793m CLIA kit Cagb,Calgranulin-B,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,Mouse,Mrp14,MRP-14,Mus musculus,p14,Protein S100-A9,S100 calcium-binding protein A9,S100a9 96T
E1793h ELISA CAGB,Calgranulin-B,Calprotectin L1H subunit,CFAG,Homo sapiens,Human,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,MRP14,MRP-14,p14,Protein S100-A9,S100 calcium- 96T
U1793h CLIA CAGB,Calgranulin-B,Calprotectin L1H subunit,CFAG,Homo sapiens,Human,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,MRP14,MRP-14,p14,Protein S100-A9,S100 calcium-b 96T
E1793h ELISA kit CAGB,Calgranulin-B,Calprotectin L1H subunit,CFAG,Homo sapiens,Human,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,MRP14,MRP-14,p14,Protein S100-A9,S100 cal 96T
U1793h CLIA kit CAGB,Calgranulin-B,Calprotectin L1H subunit,CFAG,Homo sapiens,Human,Leukocyte L1 complex heavy chain,Migration inhibitory factor-related protein 14,MRP14,MRP-14,p14,Protein S100-A9,S100 calc 96T
U1793r CLIA kit Calgranulin-B,Migration inhibitory factor-related protein 14,Mrp14,MRP-14,Myeloid-related protein 14,p14,Protein S100-A9,Rat,Rattus norvegicus,S100 calcium-binding protein A9,S100a9 96T
E1793r ELISA kit Calgranulin-B,Migration inhibitory factor-related protein 14,Mrp14,MRP-14,Myeloid-related protein 14,p14,Protein S100-A9,Rat,Rattus norvegicus,S100 calcium-binding protein A9,S100a9 96T
E1793r ELISA Calgranulin-B,Migration inhibitory factor-related protein 14,Mrp14,MRP-14,Myeloid-related protein 14,p14,Protein S100-A9,Rat,Rattus norvegicus,S100 calcium-binding protein A9,S100a9 96T
U1793r CLIA Calgranulin-B,Migration inhibitory factor-related protein 14,Mrp14,MRP-14,Myeloid-related protein 14,p14,Protein S100-A9,Rat,Rattus norvegicus,S100 calcium-binding protein A9,S100a9 96T
E1792r ELISA kit Calgranulin-A,Migration inhibitory factor-related protein 8,Mrp8,MRP-8,p8,Protein S100-A8,Rat,Rattus norvegicus,S100 calcium-binding protein A8,S100a8 96T
U1792r CLIA kit Calgranulin-A,Migration inhibitory factor-related protein 8,Mrp8,MRP-8,p8,Protein S100-A8,Rat,Rattus norvegicus,S100 calcium-binding protein A8,S100a8 96T
U1792r CLIA Calgranulin-A,Migration inhibitory factor-related protein 8,Mrp8,MRP-8,p8,Protein S100-A8,Rat,Rattus norvegicus,S100 calcium-binding protein A8,S100a8 96T
E1792r ELISA Calgranulin-A,Migration inhibitory factor-related protein 8,Mrp8,MRP-8,p8,Protein S100-A8,Rat,Rattus norvegicus,S100 calcium-binding protein A8,S100a8 96T
U1793Rb CLIA kit Calgranulin-B,Migration inhibitory factor-related protein 14,MRP14,MRP-14,Oryctolagus cuniculus,p14,Protein S100-A9,Rabbit,S100 calcium-binding protein A9,S100A9 96T
E1793Rb ELISA kit Calgranulin-B,Migration inhibitory factor-related protein 14,MRP14,MRP-14,Oryctolagus cuniculus,p14,Protein S100-A9,Rabbit,S100 calcium-binding protein A9,S100A9 96T
U1793Rb CLIA Calgranulin-B,Migration inhibitory factor-related protein 14,MRP14,MRP-14,Oryctolagus cuniculus,p14,Protein S100-A9,Rabbit,S100 calcium-binding protein A9,S100A9 96T
E1793Rb ELISA Calgranulin-B,Migration inhibitory factor-related protein 14,MRP14,MRP-14,Oryctolagus cuniculus,p14,Protein S100-A9,Rabbit,S100 calcium-binding protein A9,S100A9 96T
20-272-191081 MRP8 + MRP14 - Mouse monoclonal [2Q1841] to MRP8 + MRP14; S100 calcium-binding protein A8; Calgranulin-A; Migration inhibitory factor-related protein 8; MRP-8; Cystic fibrosis antigen; CFAG; P8; Leuko 0.05 mg


 

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