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

Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1 (Protein ABNORMAL INFLORESCENCE MERISTEM 1) (AtAIM1) [Includes: Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]

 AIM1_ARATH              Reviewed;         721 AA.
Q9ZPI6;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-APR-2018, entry version 141.
RecName: Full=Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1;
AltName: Full=Protein ABNORMAL INFLORESCENCE MERISTEM 1;
Short=AtAIM1;
Includes:
RecName: Full=Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
EC=4.2.1.17;
EC=5.1.2.3;
EC=5.3.3.8;
Includes:
RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.35;
Name=AIM1; OrderedLocusNames=At4g29010; ORFNames=F19B15.40;
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=10521521; DOI=10.1105/tpc.11.10.1911;
Richmond T.A., Bleecker A.B.;
"A defect in beta-oxidation causes abnormal inflorescence development
in Arabidopsis.";
Plant Cell 11:1911-1924(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
FUNCTION.
PubMed=17544464; DOI=10.1016/j.phytochem.2007.04.024;
Delker C., Zolman B.K., Miersch O., Wasternack C.;
"Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal
beta-oxidation enzymes--additional proof by properties of pex6 and
aim1.";
Phytochemistry 68:1642-1650(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[7]
FUNCTION.
PubMed=20463021; DOI=10.1074/jbc.M110.106005;
Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.;
"The multifunctional protein in peroxisomal beta-oxidation: structure
and substrate specificity of the Arabidopsis thaliana protein MFP2.";
J. Biol. Chem. 285:24066-24077(2010).
[8]
FUNCTION.
PubMed=24254312; DOI=10.1104/pp.113.229807;
Bussell J.D., Reichelt M., Wiszniewski A.A., Gershenzon J.,
Smith S.M.;
"Peroxisomal ATP-binding cassette transporter COMATOSE and the
multifunctional protein abnormal INFLORESCENCE MERISTEM are required
for the production of benzoylated metabolites in Arabidopsis seeds.";
Plant Physiol. 164:48-54(2014).
-!- FUNCTION: Involved in peroxisomal fatty acid beta-oxidation.
Required for wound-induced jasmonate biosynthesis. Possesses
enoyl-CoA hydratase activity against short chain substrates (C4-
C6) and 3-hydroxyacyl-CoA dehydrogenase activity against chains of
variable sizes (C6-C16) (PubMed:10521521, PubMed:17544464,
PubMed:20463021). Possesses cinnamoyl-CoA hydratase activity and
is involved in the peroxisomal beta-oxidation pathway for the
biosynthesis of benzoic acid (BA). Required for the accumulation
in seeds of benzoylated glucosinolates (BGs) and substituted
hydroxybenzoylated choline esters, which are BA-containing
secondary metabolites. Required for salicylic acid (SA) in seeds
(PubMed:24254312). {ECO:0000269|PubMed:10521521,
ECO:0000269|PubMed:17544464, ECO:0000269|PubMed:20463021,
ECO:0000269|PubMed:24254312}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O.
-!- CATALYTIC ACTIVITY: A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-
CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
hydroxybutanoyl-CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=115 uM for crotonyl-CoA {ECO:0000269|PubMed:10521521};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10521521}.
-!- DOMAIN: The epimerase and isomerase activities are contained in
the N-terminal region while the dehydrogenase activity is in the
C-terminal region. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Reduced rosette size, twisted leaves, and
abnormal and sterile flowers. {ECO:0000269|PubMed:10521521}.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CoA dehydrogenase 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; AF123253; AAD18041.1; -; Genomic_DNA.
EMBL; AL078470; CAB43915.1; -; Genomic_DNA.
EMBL; AL161574; CAB79659.1; -; Genomic_DNA.
EMBL; CP002687; AEE85572.1; -; Genomic_DNA.
EMBL; AY059815; AAL24297.1; -; mRNA.
EMBL; AY072072; AAL59895.1; -; mRNA.
EMBL; AY096659; AAM20293.1; -; mRNA.
PIR; T08956; T08956.
RefSeq; NP_194630.1; NM_119045.5.
UniGene; At.3404; -.
UniGene; At.48915; -.
ProteinModelPortal; Q9ZPI6; -.
SMR; Q9ZPI6; -.
BioGrid; 14309; 1.
STRING; 3702.AT4G29010.1; -.
SwissLipids; SLP:000000866; -.
iPTMnet; Q9ZPI6; -.
PaxDb; Q9ZPI6; -.
PRIDE; Q9ZPI6; -.
EnsemblPlants; AT4G29010.1; AT4G29010.1; AT4G29010.
GeneID; 829022; -.
Gramene; AT4G29010.1; AT4G29010.1; AT4G29010.
KEGG; ath:AT4G29010; -.
Araport; AT4G29010; -.
TAIR; locus:2119891; AT4G29010.
eggNOG; KOG1683; Eukaryota.
eggNOG; COG1024; LUCA.
eggNOG; COG1250; LUCA.
HOGENOM; HOG000261347; -.
InParanoid; Q9ZPI6; -.
KO; K10527; -.
OMA; PAIKRAH; -.
OrthoDB; EOG09360359; -.
PhylomeDB; Q9ZPI6; -.
BioCyc; MetaCyc:AT4G29010-MONOMER; -.
Reactome; R-ATH-390247; Beta-oxidation of very long chain fatty acids.
SABIO-RK; Q9ZPI6; -.
UniPathway; UPA00659; -.
PRO; PR:Q9ZPI6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9ZPI6; baseline and differential.
Genevisible; Q9ZPI6; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; ISS:TAIR.
GO; GO:0009908; P:flower development; IMP:TAIR.
GO; GO:0009695; P:jasmonic acid biosynthetic process; IMP:UniProtKB.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR033346; AIM1.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23309:SF10; PTHR23309:SF10; 1.
Pfam; PF00725; 3HCDH; 1.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
Complete proteome; Fatty acid metabolism; Isomerase; Lipid metabolism;
Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome;
Reference proteome.
CHAIN 1 721 Peroxisomal fatty acid beta-oxidation
multifunctional protein AIM1.
/FTId=PRO_0000401372.
MOTIF 719 721 Microbody targeting signal.
{ECO:0000305}.
ACT_SITE 116 116 Nucleophile. {ECO:0000255}.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255}.
SEQUENCE 721 AA; 77858 MW; F72FB3252B2216CF CRC64;
MAKKIGVTME VGNDGVAVIT ISNPPVNSLA SPIISGLKEK FRDANQRNDV KAIVLIGNNG
RFSGGFDINV FQQVHKTGDL SLMPEVSVEL VCNLMEDSRK PVVAAVEGLA LGGGLELAMA
CHARVAAPKA QLGLPELTLG VIPGFGGTQR LPRLVGLAKA TDMILLSKSI SSEEGHKLGL
IDALVPPGDV LSTSRKWALD IAEGRKPFLQ SLHRTDKIGS LSEARAILKN SRQLAKKIAP
NMPQHHACIE VIEEGIIHGG YSGVLKEAEV FKQLVLSDTA KGLVHVFFAQ RATSKVPNVT
DVGLKPRPIK KVAVIGGGLM GSGIATALLL SNIRVVLKEI NSEFLMKGIK SVEANMKSLV
SRGKLTQDKA GKALSLFKGV LDYTEFNDVD MVIEAVIENI QLKQNIFKEI EKVCSPHCIL
ASNTSTIDLD VIGEKTNSKD RIVGAHFFSP AHLMPLLEIV RSKNTSAQVI LDLMAVGKAI
KKVPVVVGNC IGFAVNRTFF PYSQAAHMLA NLGVDLFRID SVITSFGLPL GPFQLGDLAG
HGIGLAVGPI YAKVYGDRMF RSPMTELLLK SGRNGKINGR GYYIYEKGSK PKPDPSVLSI
VEKSRKLTNI MPGGKPISVT DKEIVEMILF PVVNEACRVL DEGVVIRASD LDIASVLGMS
FPSYRGGIVF WADTVGPKYI YERLKKLSET YGSFFKPSRY LEERAMNGML LSESKSSRSK
L


Related products :

Catalog number Product name Quantity
26-068 ECHS1 functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The prote 0.05 mg
EIAAB12380 D3,D2-enoyl-CoA isomerase,Delta(3),delta(2)-enoyl-CoA isomerase,Dodecenoyl-CoA isomerase,Eci2,Enoyl-CoA delta isomerase 2, mitochondrial,Mouse,Mus musculus,pECI,Peci,Peroxisomal 3,2-trans-enoyl-CoA is
EIAAB12381 D3,D2-enoyl-CoA isomerase,Delta(3),delta(2)-enoyl-CoA isomerase,Dodecenoyl-CoA isomerase,Eci2,Enoyl-CoA delta isomerase 2, mitochondrial,pECI,Peci,Peroxisomal 3,2-trans-enoyl-CoA isomerase,Rat,Rattus
30-102 ECHS1 functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. ECHS1 is 0.1 mg
30-101 ECHS1 functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. ECHS1 is 0.1 mg
EIAAB12378 3,2-trans-enoyl-CoA isomerase,D3,D2-enoyl-CoA isomerase,DCI,Delta(3),Delta(2)-enoyl-CoA isomerase,Dodecenoyl-CoA isomerase,ECI1,Enoyl-CoA delta isomerase 1, mitochondrial,Homo sapiens,Human
EIAAB12379 3,2-trans-enoyl-CoA isomerase,D3,D2-enoyl-CoA isomerase,Dci,Delta(3),Delta(2)-enoyl-CoA isomerase,Dodecenoyl-CoA isomerase,Eci1,Enoyl-CoA delta isomerase 1, mitochondrial,Rat,Rattus norvegicus
EIAAB12377 3,2-trans-enoyl-CoA isomerase,D3,D2-enoyl-CoA isomerase,Dci,Delta(3),Delta(2)-enoyl-CoA isomerase,Dodecenoyl-CoA isomerase,Eci1,Enoyl-CoA delta isomerase 1, mitochondrial,Mouse,Mus musculus
EIAAB12372 ECHS1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Homo sapiens,Human,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12371 Bos taurus,Bovine,ECHS1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12370 Echs1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Rat,Rattus norvegicus,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12373 Echs1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Mouse,Mus musculus,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12382 D3,D2-enoyl-CoA isomerase,DBI-related protein 1,Delta(3),delta(2)-enoyl-CoA isomerase,Diazepam-binding inhibitor-related protein 1,Dodecenoyl-CoA isomerase,DRS1,DRS-1,ECI2,Enoyl-CoA delta isomerase 2,
ECH1-2812H Protein Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal, His-tagged 0.5mg
ECH1-2812H Protein: Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal, His-tagged 0.5mg
orb90214 Human Peroxisomal D3,D2-Enoyl-CoA Isomerase protein Enzymes 5
EIAAB11110 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,Edh17b4,Hsd17b4,MFE-2,MPF-2,Multifunctional protein 2,Peroxisomal multifunctional enzyme type 2,Rat,Rattus norvegicus
EIAAB11111 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,Edh17b4,Hsd17b4,MFE-2,Mouse,MPF-2,Multifunctional protein 2,Mus musculus,Peroxisomal multifunctional enzyme type 2
EIAAB11109 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,EDH17B4,Homo sapiens,HSD17B4,Human,MFE-2,MPF-2,Multifunctional protein 2,Peroxisomal multifunctional enzyme type 2
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 5
REN-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 5
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 20
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 1mg
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal ECH1 1mg
7-02707 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 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