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

Glutathione S-transferase F2 (AtGSTF2) (EC 2.5.1.18) (24 kDa auxin-binding protein) (AtPM24) (GST class-phi member 2)

 GSTF2_ARATH             Reviewed;         212 AA.
P46422;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUL-2017, entry version 148.
RecName: Full=Glutathione S-transferase F2;
Short=AtGSTF2;
EC=2.5.1.18;
AltName: Full=24 kDa auxin-binding protein;
Short=AtPM24;
AltName: Full=GST class-phi member 2;
Name=GSTF2; Synonyms=PM24.1; OrderedLocusNames=At4g02520;
ORFNames=T10P11.18;
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], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8290582; DOI=10.1073/pnas.91.2.689;
Zettl R., Schell J., Palme K.;
"Photoaffinity labeling of Arabidopsis thaliana plasma membrane
vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a
glutathione S-transferase.";
Proc. Natl. Acad. Sci. U.S.A. 91:689-693(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY ETHYLENE.
TISSUE=Leaf;
PubMed=8329687; DOI=10.1007/BF00015980;
Zhou J., Goldsbrough P.B.;
"An Arabidopsis gene with homology to glutathione S-transferases is
regulated by ethylene.";
Plant Mol. Biol. 22:517-523(1993).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
FUNCTION, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
PubMed=12090627; DOI=10.1023/A:1015557300450;
Wagner U., Edwards R., Dixon D.P., Mauch F.;
"Probing the diversity of the Arabidopsis glutathione S-transferase
gene family.";
Plant Mol. Biol. 49:515-532(2002).
[7]
INDUCTION.
PubMed=12881503; DOI=10.1093/pcp/pcg093;
Lieberherr D., Wagner U., Dubuis P.H., Metraux J.P., Mauch F.;
"The rapid induction of glutathione S-transferases AtGSTF2 and AtGSTF6
by avirulent Pseudomonas syringae is the result of combined salicylic
acid and ethylene signaling.";
Plant Cell Physiol. 44:750-757(2003).
[8]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=14617075; DOI=10.1046/j.1365-313X.2003.01890.x;
Smith A.P., Nourizadeh S.D., Peer W.A., Xu J., Bandyopadhyay A.,
Murphy A.S., Goldsbrough P.B.;
"Arabidopsis AtGSTF2 is regulated by ethylene and auxin, and encodes a
glutathione S-transferase that interacts with flavonoids.";
Plant J. 36:433-442(2003).
[9]
INDUCTION BY COPPER.
PubMed=15069083; DOI=10.1074/jbc.M402807200;
Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E.,
Goldsbrough P.B.;
"Proteomic analysis of Arabidopsis glutathione S-transferases from
benoxacor- and copper-treated seedlings.";
J. Biol. Chem. 279:26098-26104(2004).
[10]
INDUCTION.
PubMed=15923336; DOI=10.1104/pp.104.056168;
Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L.,
Schnoor J.L.;
"Gene expression and microscopic analysis of Arabidopsis exposed to
chloroacetanilide herbicides and explosive compounds. A
phytoremediation approach.";
Plant Physiol. 138:858-869(2005).
[11]
SUBCELLULAR LOCATION.
PubMed=19174456; DOI=10.1093/jxb/ern365;
Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
"Enzyme activities and subcellular localization of members of the
Arabidopsis glutathione transferase superfamily.";
J. Exp. Bot. 60:1207-1218(2009).
[12]
FUNCTION.
PubMed=21631432; DOI=10.1042/BJ20101884;
Dixon D.P., Sellars J.D., Edwards R.;
"The Arabidopsis phi class glutathione transferase AtGSTF2: binding
and regulation by biologically active heterocyclic ligands.";
Biochem. J. 438:63-70(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
HEXYLGLUTATHIONE.
PubMed=8551521; DOI=10.1006/jmbi.1996.0024;
Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R.,
Palme K., Schell J., Koelln I., Bartunik H.D., Bieseler B.;
"Three-dimensional structure of glutathione S-transferase from
Arabidopsis thaliana at 2.2-A resolution: structural characterization
of herbicide-conjugating plant glutathione S-transferases and a novel
active site architecture.";
J. Mol. Biol. 255:289-309(1996).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
ANALOG.
PubMed=9817846; DOI=10.1016/S0969-2126(98)00143-9;
Prade L., Huber R., Bieseler B.;
"Structures of herbicides in complex with their detoxifying enzyme
glutathione S-transferase -- explanations for the selectivity of the
enzyme in plants.";
Structure 6:1445-1452(1998).
-!- FUNCTION: Binds auxin, endogenous flavonoids and the phytoalexin
camalexin and may be involved in regulating the binding and
transport of small bioactive natural products and defense-related
compounds during plant stress. Binds a series of heterocyclic
compounds, including lumichrome, harmane, norharmane and indole-3-
aldehyde. In vitro, possesses glutathione S-transferase activity
toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl
isothiocyanate (BITC). Acts as glutathione peroxidase on cumene
hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene
oxide, but not trans-cinnamic acid or IAA-CoA.
{ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:21631432}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8551521,
ECO:0000269|PubMed:9817846}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19174456}. Microsome
{ECO:0000269|PubMed:19174456}. Endoplasmic reticulum
{ECO:0000269|PubMed:19174456}. Note=Plasma membrane vesicles.
-!- TISSUE SPECIFICITY: Expressed in the root-shoot transition zone
and root tips. {ECO:0000269|PubMed:14617075}.
-!- INDUCTION: By ethylene, auxin, glutathione, salicylic acid,
copper, paraquat, acetochlor, metolachlor and the pathogens
P.syringae and Hyaloperonospora parasitica.
{ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:12881503,
ECO:0000269|PubMed:14617075, ECO:0000269|PubMed:15069083,
ECO:0000269|PubMed:15923336, ECO:0000269|PubMed:8329687}.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X75303; CAA53051.1; -; mRNA.
EMBL; L07589; AAA32800.1; -; mRNA.
EMBL; L11601; AAA32801.1; -; mRNA.
EMBL; AC002330; AAC78264.1; -; Genomic_DNA.
EMBL; AL161494; CAB80745.1; -; Genomic_DNA.
EMBL; CP002687; AEE82183.1; -; Genomic_DNA.
EMBL; AF324681; AAG40032.1; -; mRNA.
EMBL; AF326903; AAG41485.1; -; mRNA.
EMBL; AF349527; AAK15574.1; -; mRNA.
EMBL; AY039580; AAK62635.1; -; mRNA.
EMBL; AY056082; AAL06970.1; -; mRNA.
PIR; S35268; S35268.
RefSeq; NP_192161.1; NM_116486.3.
UniGene; At.22195; -.
UniGene; At.24972; -.
PDB; 1BX9; X-ray; 2.60 A; A=2-212.
PDB; 1GNW; X-ray; 2.20 A; A/B=2-212.
PDB; 5A4U; X-ray; 2.00 A; A/B/C/D/E/F=1-212.
PDB; 5A4V; X-ray; 2.38 A; A/B/C/D/E/F=1-212.
PDB; 5A4W; X-ray; 2.25 A; A/B/C/D/E/F=1-212.
PDB; 5A5K; X-ray; 2.77 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-212.
PDBsum; 1BX9; -.
PDBsum; 1GNW; -.
PDBsum; 5A4U; -.
PDBsum; 5A4V; -.
PDBsum; 5A4W; -.
PDBsum; 5A5K; -.
ProteinModelPortal; P46422; -.
SMR; P46422; -.
BioGrid; 13222; 7.
STRING; 3702.AT4G02520.1; -.
iPTMnet; P46422; -.
SWISS-2DPAGE; P46422; -.
PaxDb; P46422; -.
PRIDE; P46422; -.
EnsemblPlants; AT4G02520.1; AT4G02520.1; AT4G02520.
GeneID; 827931; -.
Gramene; AT4G02520.1; AT4G02520.1; AT4G02520.
KEGG; ath:AT4G02520; -.
Araport; AT4G02520; -.
TAIR; locus:2132308; AT4G02520.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125746; -.
InParanoid; P46422; -.
KO; K00799; -.
OMA; PHWLENP; -.
OrthoDB; EOG09360M18; -.
PhylomeDB; P46422; -.
BioCyc; ARA:AT4G02520-MONOMER; -.
EvolutionaryTrace; P46422; -.
PRO; PR:P46422; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P46422; baseline and differential.
Genevisible; P46422; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:2001147; F:camalexin binding; IDA:TAIR.
GO; GO:0043295; F:glutathione binding; IDA:TAIR.
GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:2001227; F:quercitrin binding; IDA:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
CDD; cd03187; GST_C_Phi; 1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR034347; GST_Phi_C.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Complete proteome; Cytoplasm;
Detoxification; Direct protein sequencing; Endoplasmic reticulum;
Microsome; Oxidoreductase; Peroxidase; Plant defense;
Reference proteome; Stress response; Transferase.
CHAIN 1 212 Glutathione S-transferase F2.
/FTId=PRO_0000185848.
DOMAIN 2 83 GST N-terminal.
DOMAIN 93 212 GST C-terminal.
REGION 12 13 Glutathione binding.
REGION 41 42 Glutathione binding.
REGION 54 55 Glutathione binding.
REGION 67 68 Glutathione binding.
STRAND 4 8 {ECO:0000244|PDB:5A4U}.
HELIX 13 24 {ECO:0000244|PDB:5A4U}.
STRAND 30 33 {ECO:0000244|PDB:5A4U}.
HELIX 36 38 {ECO:0000244|PDB:5A4U}.
HELIX 40 42 {ECO:0000244|PDB:5A4U}.
HELIX 46 49 {ECO:0000244|PDB:5A4U}.
STRAND 57 60 {ECO:0000244|PDB:5A4U}.
STRAND 63 67 {ECO:0000244|PDB:5A4U}.
HELIX 68 78 {ECO:0000244|PDB:5A4U}.
TURN 79 81 {ECO:0000244|PDB:5A4U}.
STRAND 82 84 {ECO:0000244|PDB:5A4U}.
HELIX 94 109 {ECO:0000244|PDB:5A4U}.
HELIX 112 122 {ECO:0000244|PDB:5A4U}.
HELIX 124 127 {ECO:0000244|PDB:5A4U}.
HELIX 134 157 {ECO:0000244|PDB:5A4U}.
STRAND 158 160 {ECO:0000244|PDB:5A4V}.
STRAND 163 165 {ECO:0000244|PDB:5A4U}.
HELIX 168 171 {ECO:0000244|PDB:5A4U}.
HELIX 174 180 {ECO:0000244|PDB:5A4U}.
HELIX 186 190 {ECO:0000244|PDB:5A4U}.
HELIX 193 204 {ECO:0000244|PDB:5A4U}.
HELIX 206 211 {ECO:0000244|PDB:5A4U}.
SEQUENCE 212 AA; 24129 MW; 90A1CBEEEBAC815B CRC64;
MAGIKVFGHP ASIATRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN PFGQVPAFED
GDLKLFESRA ITQYIAHRYE NQGTNLLQTD SKNISQYAIM AIGMQVEDHQ FDPVASKLAF
EQIFKSIYGL TTDEAVVAEE EAKLAKVLDV YEARLKEFKY LAGETFTLTD LHHIPAIQYL
LGTPTKKLFT ERPRVNEWVA EITKRPASEK VQ


Related products :

Catalog number Product name Quantity
E0609m ELISA Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
U0609m CLIA Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
E0609m ELISA Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
U0609m CLIA Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
E0609h ELISA kit Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609h ELISA Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
E0609h ELISA Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609h ELISA Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
E0609m ELISA Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
E0609h ELISA kit Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
U0609h CLIA Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
U0609h CLIA Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
E0609m ELISA kit Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
U0609h CLIA Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
E0609h ELISA kit Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
U0609m CLIA Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
E0609m ELISA Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
U0609m CLIA Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
E0609b ELISA kit Bos taurus,Bovine,Glutathione S-transferase A4,Glutathione S-transferase alpha-4,GST class-alpha member 4,GSTA4 96T
E0609b ELISA kit Bos taurus,Bovine,Glutathione S-transferase A1,Glutathione S-transferase alpha-1,GST class-alpha member 1,GSTA1 96T
U0609b CLIA Bos taurus,Bovine,Glutathione S-transferase A2,Glutathione S-transferase alpha-2,GST class-alpha member 2,GSTA2 96T
U0609b CLIA Bos taurus,Bovine,Glutathione S-transferase A1,Glutathione S-transferase alpha-1,GST class-alpha member 1,GSTA1 96T


 

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