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

Aromatic aminotransferase ISS1 (EC 2.6.1.27) (EC 2.6.1.5) (EC 2.6.1.88) (Methionine aminotransferase ISS1) (Phenylalanine aminotransferase ISS1) (Protein INDOLE SEVERE SENSITIVE 1) (Protein REVERSAL OF SAV3 PHENOTYPE 1) (Tryptophan aminotransferase ISS1) (Tyrosine aminotransferase ISS1)

 ISS1_ARATH              Reviewed;         394 AA.
Q9C969;
07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
30-AUG-2017, entry version 118.
RecName: Full=Aromatic aminotransferase ISS1 {ECO:0000303|PubMed:26163189};
EC=2.6.1.27 {ECO:0000269|PubMed:26163189};
EC=2.6.1.5 {ECO:0000269|PubMed:26163189};
EC=2.6.1.88 {ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189};
AltName: Full=Methionine aminotransferase ISS1 {ECO:0000305};
AltName: Full=Phenylalanine aminotransferase ISS1 {ECO:0000305};
AltName: Full=Protein INDOLE SEVERE SENSITIVE 1 {ECO:0000303|PubMed:26163189};
AltName: Full=Protein REVERSAL OF SAV3 PHENOTYPE 1 {ECO:0000303|PubMed:23377040};
AltName: Full=Tryptophan aminotransferase ISS1 {ECO:0000305};
AltName: Full=Tyrosine aminotransferase ISS1 {ECO:0000305};
Name=ISS1 {ECO:0000303|PubMed:26163189};
Synonyms=VAS1 {ECO:0000303|PubMed:23377040};
OrderedLocusNames=At1g80360 {ECO:0000312|Araport:AT1G80360};
ORFNames=F5I6.11 {ECO:0000312|EMBL:AAG52437.1};
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 [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).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[5]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-66; LEU-77;
GLY-179; CYS-219 AND ALA-269, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=23377040; DOI=10.1038/nchembio.1178;
Zheng Z., Guo Y., Novak O., Dai X., Zhao Y., Ljung K., Noel J.P.,
Chory J.;
"Coordination of auxin and ethylene biosynthesis by the
aminotransferase VAS1.";
Nat. Chem. Biol. 9:244-246(2013).
[6]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-362, AND CATALYTIC
ACTIVITY.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=26163189; DOI=10.1534/genetics.115.180356;
Pieck M., Yuan Y., Godfrey J., Fisher C., Zolj S., Vaughan D.,
Thomas N., Wu C., Ramos J., Lee N., Normanly J., Celenza J.L.;
"Auxin and tryptophan homeostasis are facilitated by the ISS1/VAS1
aromatic aminotransferase in Arabidopsis.";
Genetics 201:185-199(2015).
-!- FUNCTION: Coordinates and prevents auxin (IAA) and ethylene
biosynthesis, thus regulating auxin homeostasis in young seedlings
(PubMed:23377040, PubMed:26163189). Shows aminotransferase
activity with methionine; can use the ethylene biosynthetic
intermediate L-methionine (L-Met) as an amino donor and the auxin
biosynthetic intermediate, indole-3-pyruvic acid (3-IPA) as an
amino acceptor to produce L-tryptophan (L-Trp) and 2-oxo-4-
methylthiobutyric acid (KMBA) (PubMed:23377040). Can also use
tryptophan (Trp), phenylalanine (Phe), and tyrosine (Tyr) as
substrates. Regulates tryptophan (Trp) homeostasis and catabolism
in mature plants. Also possibly involved in the metabolism of
other aromatic amino acids and phenylpropanoid homeostasis
(PubMed:26163189). {ECO:0000269|PubMed:23377040,
ECO:0000269|PubMed:26163189}.
-!- CATALYTIC ACTIVITY: L-methionine + a 2-oxo acid = 2-oxo-4-
methylthiobutanoate + an L-amino acid.
{ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189}.
-!- CATALYTIC ACTIVITY: L-tryptophan + 2-oxoglutarate = (indol-3-
yl)pyruvate + L-glutamate. {ECO:0000269|PubMed:26163189}.
-!- CATALYTIC ACTIVITY: L-tyrosine + 2-oxoglutarate = 4-
hydroxyphenylpyruvate + L-glutamate.
{ECO:0000269|PubMed:26163189}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P00509};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=70 uM for indole-3-pyruvic acid (at pH 8.5 and 37 degrees
Celsius) {ECO:0000269|PubMed:23377040};
KM=630 uM for L-Met (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:23377040};
KM=2600 uM for L-Phe (at pH 8.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:23377040};
Vmax=1 umol/min/ug enzyme with indole-3-pyruvic acid as
substrate (at pH 8 and 23 degrees Celsius)
{ECO:0000269|PubMed:23377040};
Vmax=0.82 umol/min/ug enzyme with L-Met as substrate (at pH 8
and 23 degrees Celsius) {ECO:0000269|PubMed:23377040};
Vmax=0.14 umol/min/ug enzyme with L-Phe as substrate (at pH 8
and 23 degrees Celsius) {ECO:0000269|PubMed:23377040};
Note=kcat is 2.5 min(-1) with indole-3-pyruvic acid as
substrate. kcat is 1.9 min(-1) with L-Met as substrate. kcat is
3.16 min(-1) with L-Phe as substrate (at pH 8.5 and 37 degrees
Celsius). {ECO:0000269|PubMed:23377040};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00509}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23377040}.
-!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and flowers.
{ECO:0000269|PubMed:23377040}.
-!- DISRUPTION PHENOTYPE: Suppressor of sav3 mutant plants leading to
rescued hypocotyl elongation in response to shade and restored
auxin biosynthetic pathway. In continuous white light, elongated
hypocotyls and petioles, with increased leaf hyponasty, decreased
leaf area, and accelerated leaf senescence as well as early
flowering. Increases levels of auxin (IAA), indole-3-pyruvic acid
(3-IPA) and the ethylene precursor 1-aminocyclopropane-1-
carboxylate (ACC) (PubMed:23377040). Indole-dependent auxin (IAA)
overproduction phenotypes including leaf epinasty and adventitious
rooting. In contrast to normal plants, uses primarily Trp-
independent (Trp-I) IAA synthesis when grown on indole-
supplemented medium, but uses primarily Trp-dependent (Trp-D) IAA
synthesis when grown on unsupplemented medium. Accumulates
strongly IAA and Trp when grown on indole, probably due to loss of
Trp catabolism. Altered phenylpropanoid profile (PubMed:26163189).
{ECO:0000269|PubMed:23377040, ECO:0000269|PubMed:26163189}.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC018848; AAG52437.1; -; Genomic_DNA.
EMBL; CP002684; AEE36391.1; -; Genomic_DNA.
EMBL; CP002684; ANM59817.1; -; Genomic_DNA.
EMBL; CP002684; ANM59818.1; -; Genomic_DNA.
EMBL; CP002684; ANM59819.1; -; Genomic_DNA.
EMBL; AY093159; AAM13158.1; -; mRNA.
EMBL; BT008854; AAP68293.1; -; mRNA.
PIR; C96835; C96835.
RefSeq; NP_001322147.1; NM_001334979.1.
RefSeq; NP_001322148.1; NM_001334980.1.
RefSeq; NP_001322149.1; NM_001334981.1.
RefSeq; NP_178152.1; NM_106685.5.
UniGene; At.33916; -.
SMR; Q9C969; -.
STRING; 3702.AT1G80360.1; -.
EnsemblPlants; AT1G80360.1; AT1G80360.1; AT1G80360.
EnsemblPlants; AT1G80360.2; AT1G80360.2; AT1G80360.
EnsemblPlants; AT1G80360.3; AT1G80360.3; AT1G80360.
EnsemblPlants; AT1G80360.4; AT1G80360.4; AT1G80360.
GeneID; 844376; -.
Gramene; AT1G80360.1; AT1G80360.1; AT1G80360.
Gramene; AT1G80360.2; AT1G80360.2; AT1G80360.
Gramene; AT1G80360.3; AT1G80360.3; AT1G80360.
Gramene; AT1G80360.4; AT1G80360.4; AT1G80360.
Araport; AT1G80360; -.
TAIR; locus:2034240; AT1G80360.
eggNOG; KOG0257; Eukaryota.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000223064; -.
OMA; YFNHEMA; -.
OrthoDB; EOG09360CA5; -.
BioCyc; ARA:AT1G80360-MONOMER; -.
BioCyc; MetaCyc:AT1G80360-MONOMER; -.
Proteomes; UP000006548; Chromosome 1.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0010326; F:methionine-oxo-acid transaminase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
GO; GO:0009072; P:aromatic amino acid family metabolic process; IDA:UniProtKB.
GO; GO:0009851; P:auxin biosynthetic process; IMP:UniProtKB.
GO; GO:0010252; P:auxin homeostasis; IMP:UniProtKB.
GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
GO; GO:0006555; P:methionine metabolic process; IDA:UniProtKB.
GO; GO:0010366; P:negative regulation of ethylene biosynthetic process; IMP:TAIR.
GO; GO:1901997; P:negative regulation of indoleacetic acid biosynthetic process via tryptophan; IDA:TAIR.
GO; GO:0009698; P:phenylpropanoid metabolic process; IMP:UniProtKB.
GO; GO:0009641; P:shade avoidance; IMP:TAIR.
GO; GO:0006569; P:tryptophan catabolic process; IMP:UniProtKB.
GO; GO:0006568; P:tryptophan metabolic process; IDA:UniProtKB.
GO; GO:0006570; P:tyrosine metabolic process; IDA:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
Acetylation; Aminotransferase; Auxin biosynthesis; Complete proteome;
Cytoplasm; Ethylene biosynthesis; Phenylpropanoid metabolism;
Pyridoxal phosphate; Reference proteome; Transferase;
Tryptophan catabolism.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 394 Aromatic aminotransferase ISS1.
/FTId=PRO_0000440181.
REGION 98 99 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:O84395}.
REGION 230 232 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:O84395}.
BINDING 38 38 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P00509}.
BINDING 64 64 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:Q93ZN9}.
BINDING 123 123 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:O84395}.
BINDING 123 123 Substrate.
{ECO:0000250|UniProtKB:Q93ZN9}.
BINDING 176 176 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:O84395}.
BINDING 176 176 Substrate.
{ECO:0000250|UniProtKB:P00509}.
BINDING 207 207 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:O84395}.
BINDING 241 241 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:Q93ZN9}.
BINDING 362 362 Substrate.
{ECO:0000250|UniProtKB:Q93ZN9}.
BINDING 374 374 Substrate.
{ECO:0000250|UniProtKB:P00509}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 233 233 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:O84395}.
MUTAGEN 66 66 P->L: In vas1-4; suppressor of sav3
mutant plants leading to rescued
hypocotyl elongation in response to shade
and restored auxin biosynthetic pathway.
{ECO:0000269|PubMed:23377040}.
MUTAGEN 77 77 L->F: In vas1-5; suppressor of sav3
mutant plants leading to rescued
hypocotyl elongation in response to shade
and restored auxin biosynthetic pathway.
{ECO:0000269|PubMed:23377040}.
MUTAGEN 179 179 G->D: In vas1-2; suppressor of sav3
mutant plants leading to rescued
hypocotyl elongation in response to shade
and restored auxin biosynthetic pathway.
Increases levels of auxin (IAA) and
indole-3-pyruvic acid (3-IPA).
{ECO:0000269|PubMed:23377040}.
MUTAGEN 219 219 C->Y: In vas1-7; suppressor of sav3
mutant plants leading to rescued
hypocotyl elongation in response to shade
and restored auxin biosynthetic pathway.
{ECO:0000269|PubMed:23377040}.
MUTAGEN 269 269 A->T: In vas1-8; suppressor of sav3
mutant plants leading to rescued
hypocotyl elongation in response to shade
and restored auxin biosynthetic pathway.
{ECO:0000269|PubMed:23377040}.
MUTAGEN 362 362 R->W: In iss1-2; indole-dependent auxin
(IAA) overproduction phenotypes including
leaf epinasty and adventitious rooting.
{ECO:0000269|PubMed:26163189}.
SEQUENCE 394 AA; 43762 MW; E848C65BAB140620 CRC64;
MGSFGMLSRR TLGTDMPVMA QIRSLMAELT NPMSLAQGVV HWQPPQKALE KVKELVWDPI
ISSYGPDEGL PELRQALLKK LREENKLTNS QVMVTAGANQ AFVNLVITLC DAGDSVVMFE
PYYFNSYMAF QMTGVTNIIV GPGQSDTLYP DADWLERTLS ESKPTPKVVT VVNPGNPSGT
YVPEPLLKRI AQICKDAGCW LIVDNTYEYF MYDGLKHCCV EGDHIVNVFS FSKTYGMMGW
RLGYIAYSER LDGFATELVK IQDNIPICAA IISQRLAVYA LEEGSGWITE RVKSLVKNRD
IVKEALEPLG KENVKGGEGA IYLWAKLPEG HRDDFKVVRW LAHRHGVVVI PGCASGSPGY
LRVSFGGLQE VEMRAAAARL RKGIEELLHH GMVE


Related products :

Catalog number Product name Quantity
EIAAB28576 Homo sapiens,Human,OAT,Ornithine aminotransferase, mitochondrial,Ornithine delta-aminotransferase,Ornithine--oxo-acid aminotransferase
EIAAB37898 Endometrial progesterone-induced protein,EPIP,Oryctolagus cuniculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,PSA,PSAT,PSAT1,Rabbit
EIAAB37900 Endometrial progesterone-induced protein,EPIP,Mouse,Mus musculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,Psa,PSAT,Psat,Psat1
EIAAB37899 Homo sapiens,Human,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,PSA,PSAT,PSAT1
15-288-21256 Phosphoserine aminotransferase - EC 2.6.1.52; Phosphohydroxythreonine aminotransferase; PSAT Polyclonal 0.05 mg
15-288-21256 Phosphoserine aminotransferase - EC 2.6.1.52; Phosphohydroxythreonine aminotransferase; PSAT Polyclonal 0.1 mg
EIAAB39810 AGT,Agt1,Agxt,Alanine--glyoxylate aminotransferase,Rat,Rattus norvegicus,Serine--pyruvate aminotransferase, mitochondrial,SPT
EIAAB39808 AGT,Agxt,Agxt1,Alanine--glyoxylate aminotransferase,Mouse,Mus musculus,Serine--pyruvate aminotransferase, mitochondrial,SPT
EIAAB39809 AGT,AGT1,AGXT,Alanine--glyoxylate aminotransferase,Oryctolagus cuniculus,Rabbit,Serine--pyruvate aminotransferase,SPT
EIAAB39811 AGT,AGT1,AGXT,Alanine--glyoxylate aminotransferase,Homo sapiens,Human,Serine--pyruvate aminotransferase,SPAT,SPT
orb90202 Human Ornithine Aminotransferase protein Ornithine Aminotransferase Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and ha 5
orb90026 Human Alanine Aminotransferase protein Alanine Aminotransferase Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing having a molecular mass of 54,479 Dalto 1 U
30-187 PSAT1 is likely a phosphoserine aminotransferase, based on similarity to proteins in mouse, rabbit, and Drosophila.The protein encoded by this gene is likely a phosphoserine aminotransferase, based on 0.05 mg
EIAAB28577 Mouse,Mus musculus,Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
EIAAB28574 Oat,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase,Rat,Rattus norvegicus
EIAAB28575 Bos taurus,Bovine,OAT,Ornithine aminotransferase, mitochondrial,Ornithine--oxo-acid aminotransferase
LF-PA40002 anti-Aminoadipate Aminotransferase (AADAT) , Rabbit polyclonal to Aminoadipate Aminotransferase (AADAT) , Isotype IgG, Host Rabbit 50 ug
LF-PA40003 anti-Aminoadipate Aminotransferase (AADAT) , Rabbit polyclonal to Aminoadipate Aminotransferase (AADAT) , Isotype IgG, Host Rabbit 50 ug
46420002 TAT (Tyrosine aminotransferase) 50 µg
TAT TAT Gene tyrosine aminotransferase
H9690 Tyrosine aminotransferase(TAT), Rat, ELISA Kit 96T
'H00006898-P01-25 TAT (Tyrosine aminotransferase) antigen 25
'H00006898-P01-10 TAT (Tyrosine aminotransferase) antigen 10
CSB-EL023175RA Rat tyrosine aminotransferase (TAT) ELISA kit 96T
CSB-EL023175MO Mouse tyrosine aminotransferase (TAT) ELISA kit 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