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

Pyridoxal 5'-phosphate synthase subunit PDX1.3 (AtPDX1.3) (AtPDX1;1) (PLP synthase subunit PDX1.3) (EC 4.3.3.6)

 PDX13_ARATH             Reviewed;         309 AA.
Q8L940; Q3KRU4; Q9M032;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
05-DEC-2018, entry version 128.
RecName: Full=Pyridoxal 5'-phosphate synthase subunit PDX1.3;
Short=AtPDX1.3;
Short=AtPDX1;1;
Short=PLP synthase subunit PDX1.3;
EC=4.3.3.6 {ECO:0000269|PubMed:17468224};
Name=PDX13; Synonyms=GIP2, PDX1L3, RSR4; OrderedLocusNames=At5g01410;
ORFNames=T10O8.120;
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]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=16236150; DOI=10.1111/j.1365-313X.2005.02538.x;
Chen H., Xiong L.;
"Pyridoxine is required for post-embryonic root development and
tolerance to osmotic and oxidative stresses.";
Plant J. 44:396-408(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-54, TISSUE
SPECIFICITY, AND INTERACTION WITH PDX1.1; PDX1.2 AND PDX2.
STRAIN=cv. C24;
PubMed=16766694; DOI=10.1105/tpc.105.036269;
Wagner S., Bernhardt A., Leuendorf J.E., Drewke C., Lytovchenko A.,
Mujahed N., Gurgui C., Frommer W.B., Leistner E., Fernie A.R.,
Hellmann H.;
"Analysis of the Arabidopsis rsr4-1/pdx1-3 mutant reveals the critical
function of the PDX1 protein family in metabolism, development, and
vitamin B6 biosynthesis.";
Plant Cell 18:1722-1735(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
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).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16157873; DOI=10.1073/pnas.0506228102;
Tambasco-Studart M., Titiz O., Raschle T., Forster G., Amrhein N.,
Fitzpatrick T.B.;
"Vitamin B6 biosynthesis in higher plants.";
Proc. Natl. Acad. Sci. U.S.A. 102:13687-13692(2005).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17468224; DOI=10.1104/pp.107.096784;
Tambasco-Studart M., Tews I., Amrhein N., Fitzpatrick T.B.;
"Functional analysis of PDX2 from Arabidopsis, a glutaminase involved
in vitamin B6 biosynthesis.";
Plant Physiol. 144:915-925(2007).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
-!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from
ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and
ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-
phosphate and dihydroxyacetone phosphate as substrates, resulting
from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Also plays an indirect role in resistance to singlet oxygen-
generating photosensitizers. {ECO:0000269|PubMed:16157873,
ECO:0000269|PubMed:16236150, ECO:0000269|PubMed:17468224}.
-!- CATALYTIC ACTIVITY:
Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
+ pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
Evidence={ECO:0000269|PubMed:17468224};
-!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
biosynthesis.
-!- SUBUNIT: Homodimer or heterodimer with PDX1.1 or PDX1.2. Interacts
with PDX2. {ECO:0000269|PubMed:16766694}.
-!- INTERACTION:
Q9ZNR6:PDX12; NbExp=5; IntAct=EBI-1545956, EBI-1545987;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Membrane.
-!- TISSUE SPECIFICITY: Expressed in cotyledons, rapidly dividing root
stele tissues, stems, leaves, flowers, mature pollen, and
siliques. {ECO:0000269|PubMed:16236150,
ECO:0000269|PubMed:16766694}.
-!- INDUCTION: Not induced by cold, salt, drought or UV stress, or by
abscisic acid or jasmonic acid. {ECO:0000269|PubMed:16236150}.
-!- DISRUPTION PHENOTYPE: Plants have a lower leaf carotenoid and
chlorophyll a and b content, and are impaired both in root cell
division and in root cell elongation. Mutant rsr4-1 can be
complemented by the addition of any of the vitamin B6 vitamers,
except pyridoxal 5'-phosphate. {ECO:0000269|PubMed:16236150}.
-!- MISCELLANEOUS: Vitamin B6 is an essential quencher of singlet
oxygen in plants, that can protect cellular membranes from lipid
peroxidation.
-!- SIMILARITY: Belongs to the PdxS/SNZ 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; AY972813; AAY42123.1; -; mRNA.
EMBL; AL161746; CAB81924.1; -; Genomic_DNA.
EMBL; CP002688; AED90340.1; -; Genomic_DNA.
EMBL; CP002688; ANM69812.1; -; Genomic_DNA.
EMBL; AF428298; AAL16130.1; -; mRNA.
EMBL; AF446352; AAL48227.1; -; mRNA.
EMBL; AY097428; AAM19944.1; -; mRNA.
EMBL; AY088650; AAM66972.1; -; mRNA.
EMBL; AK227197; BAE99236.1; -; mRNA.
PIR; T48163; T48163.
RefSeq; NP_001331465.1; NM_001342589.1.
RefSeq; NP_195761.1; NM_120219.2.
UniGene; At.23386; -.
PDB; 5K2Z; X-ray; 1.80 A; A/B/C/D=1-309.
PDB; 5K3V; X-ray; 1.90 A; A/B/C/D=1-309.
PDB; 5LNR; X-ray; 1.61 A; A/B/C/D=1-309.
PDB; 5LNS; X-ray; 1.91 A; A/B/C/D=1-309.
PDB; 5LNU; X-ray; 1.73 A; A/B/C/D=1-309.
PDB; 5LNV; X-ray; 2.24 A; A/B/C/D=1-309.
PDB; 5LNW; X-ray; 1.90 A; A/B/C/D=1-309.
PDBsum; 5K2Z; -.
PDBsum; 5K3V; -.
PDBsum; 5LNR; -.
PDBsum; 5LNS; -.
PDBsum; 5LNU; -.
PDBsum; 5LNV; -.
PDBsum; 5LNW; -.
ProteinModelPortal; Q8L940; -.
SMR; Q8L940; -.
BioGrid; 17014; 6.
IntAct; Q8L940; 3.
STRING; 3702.AT5G01410.1; -.
iPTMnet; Q8L940; -.
PaxDb; Q8L940; -.
PRIDE; Q8L940; -.
DNASU; 831738; -.
EnsemblPlants; AT5G01410.1; AT5G01410.1; AT5G01410.
EnsemblPlants; AT5G01410.2; AT5G01410.2; AT5G01410.
GeneID; 831738; -.
Gramene; AT5G01410.1; AT5G01410.1; AT5G01410.
Gramene; AT5G01410.2; AT5G01410.2; AT5G01410.
KEGG; ath:AT5G01410; -.
Araport; AT5G01410; -.
TAIR; locus:2179142; AT5G01410.
eggNOG; KOG1606; Eukaryota.
eggNOG; COG0214; LUCA.
HOGENOM; HOG000227586; -.
InParanoid; Q8L940; -.
KO; K06215; -.
OMA; IGVDMID; -.
OrthoDB; EOG09360HH8; -.
PhylomeDB; Q8L940; -.
BioCyc; ARA:GQT-915-MONOMER; -.
UniPathway; UPA00245; -.
PRO; PR:Q8L940; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8L940; baseline and differential.
Genevisible; Q8L940; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0012505; C:endomembrane system; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
GO; GO:0006520; P:cellular amino acid metabolic process; IMP:TAIR.
GO; GO:0015994; P:chlorophyll metabolic process; IMP:TAIR.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
GO; GO:0006982; P:response to lipid hydroperoxide; IMP:TAIR.
GO; GO:0010335; P:response to non-ionic osmotic stress; IMP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0010224; P:response to UV-B; IGI:TAIR.
CDD; cd04727; pdxS; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01824; PdxS; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR001852; PdxS/SNZ.
InterPro; IPR033755; PdxS/SNZ_N.
InterPro; IPR011060; RibuloseP-bd_barrel.
PANTHER; PTHR31829; PTHR31829; 1.
Pfam; PF01680; SOR_SNZ; 1.
PIRSF; PIRSF029271; Pdx1; 1.
SUPFAM; SSF51366; SSF51366; 1.
TIGRFAMs; TIGR00343; TIGR00343; 1.
PROSITE; PS01235; PDXS_SNZ_1; 1.
PROSITE; PS51129; PDXS_SNZ_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Cytoplasm; Lyase; Membrane; Pyridoxal phosphate; Reference proteome;
Schiff base.
CHAIN 1 309 Pyridoxal 5'-phosphate synthase subunit
PDX1.3.
/FTId=PRO_0000109368.
REGION 251 252 D-ribose 5-phosphate binding.
{ECO:0000250|UniProtKB:O59080}.
ACT_SITE 97 97 Schiff-base intermediate with D-ribose 5-
phosphate.
{ECO:0000250|UniProtKB:O59080}.
BINDING 40 40 D-ribose 5-phosphate.
{ECO:0000250|UniProtKB:O59080}.
BINDING 169 169 D-ribose 5-phosphate; via amide nitrogen.
{ECO:0000250|UniProtKB:O59080}.
BINDING 181 181 Glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:Q03148}.
BINDING 230 230 D-ribose 5-phosphate; via amide nitrogen.
{ECO:0000250|UniProtKB:O59080}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 54 54 G->S: In rsr4-1; strongly reduced
oligomerization and 63% reduction in
pyridoxal biosynthesis.
{ECO:0000269|PubMed:16766694}.
CONFLICT 226 226 F -> S (in Ref. 6; AAM66972).
{ECO:0000305}.
HELIX 22 30 {ECO:0000244|PDB:5LNR}.
HELIX 31 33 {ECO:0000244|PDB:5LNR}.
STRAND 36 43 {ECO:0000244|PDB:5LNR}.
HELIX 44 52 {ECO:0000244|PDB:5LNR}.
STRAND 56 60 {ECO:0000244|PDB:5LNR}.
HELIX 65 70 {ECO:0000244|PDB:5LNR}.
HELIX 80 89 {ECO:0000244|PDB:5LNR}.
STRAND 94 99 {ECO:0000244|PDB:5LNR}.
HELIX 103 112 {ECO:0000244|PDB:5LNR}.
STRAND 115 120 {ECO:0000244|PDB:5LNR}.
HELIX 134 136 {ECO:0000244|PDB:5LNR}.
STRAND 141 147 {ECO:0000244|PDB:5LNR}.
HELIX 148 157 {ECO:0000244|PDB:5LNR}.
STRAND 160 164 {ECO:0000244|PDB:5LNR}.
STRAND 168 170 {ECO:0000244|PDB:5LNU}.
HELIX 174 192 {ECO:0000244|PDB:5LNR}.
HELIX 195 197 {ECO:0000244|PDB:5LNR}.
HELIX 198 205 {ECO:0000244|PDB:5LNR}.
HELIX 209 218 {ECO:0000244|PDB:5LNR}.
STRAND 222 227 {ECO:0000244|PDB:5LNR}.
HELIX 234 243 {ECO:0000244|PDB:5LNR}.
STRAND 246 250 {ECO:0000244|PDB:5LNR}.
HELIX 253 256 {ECO:0000244|PDB:5LNR}.
STRAND 257 259 {ECO:0000244|PDB:5LNS}.
HELIX 260 272 {ECO:0000244|PDB:5LNR}.
TURN 273 275 {ECO:0000244|PDB:5LNR}.
HELIX 277 284 {ECO:0000244|PDB:5LNR}.
SEQUENCE 309 AA; 33216 MW; E74EBBCD4F124456 CRC64;
MEGTGVVAVY GNGAITEAKK SPFSVKVGLA QMLRGGVIMD VVNAEQARIA EEAGACAVMA
LERVPADIRA QGGVARMSDP QMIKEIKQAV TIPVMAKARI GHFVEAQILE AIGIDYIDES
EVLTLADEDH HINKHNFRIP FVCGCRNLGE ALRRIREGAA MIRTKGEAGT GNIIEAVRHV
RSVNGDIRVL RNMDDDEVFT FAKKLAAPYD LVMQTKQLGR LPVVQFAAGG VATPADAALM
MQLGCDGVFV GSGIFKSGDP ARRARAIVQA VTHYSDPEML VEVSCGLGEA MVGINLNDEK
VERFANRSE


Related products :

Catalog number Product name Quantity
PDX1 PDSS1 Gene prenyl (decaprenyl) diphosphate synthase, subunit 1
EIAAB11782 Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,DPM3,Homo sapiens,
EIAAB11783 Bos taurus,Bovine,Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,
EIAAB11781 Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,Dpm3,Mannose-P-dol
EIAAB11864 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,Dps1,Mouse,Mus musculus,Pdss1,Solanesyl-diphosphate synthase s
EIAAB11424 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Mouse,Mus musculus,Pdss2,Solanesyl-diphosphate synthase s
EIAAB11423 All-trans-decaprenyl-diphosphate synthase subunit 2,C6orf210,Candidate tumor suppressor protein,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,DLP1,Homo sapiens,
EIAAB11422 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Pdss2,Rat,Rattus norvegicus
EIAAB11863 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,DPS1,Homo sapiens,Human,PDSS1,TPRT,TPT 1,Trans-prenyltransfera
25-595 ATP5G2 is a subunit of mitochondrial ATP synthase. ATP synthase is composed of two linked multi-subunit complexes the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising t 0.05 mg
AS10 1590 Antibody: AtpD | CF1 delta subunit of ATP synthase, Affinity purified, Immunogen: isolated CF1 subunit of the chloroplast ATP synthase complex from Chlamydomonas reinhardtii Q42687.1, Host: rabbit, po 100 ul
AS10 1586 Antibody: AtpE | epsilon subunit of ATP synthase , Immunogen: isolated CF1 subunit of the chloroplast ATP synthase complex from Chlamydomonas reinhardtii, Host: rabbit, polyclonal, Confirmed reactivit 100 ul
AS10 1591 Antibody: AtpD | CF1 delta subunit of ATP synthase, Serum, Immunogen: isolated CF1 subunit of the chloroplast ATP synthase complex from Spinacia oleracea P11402.2, Host: rabbit, polyclonal, Confirmed 100 ul
AS10 1583 Antibody: AtpI | CFoIV subunit of ATP synthase , Immunogen: isolated CF0IV subunit of the chloroplast ATP synthase complex, Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis thaliana, Nicoti 100 ul
15-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 Polyclonal 0.1 mg
15-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 Polyclonal 0.05 mg
AS08 312 Antibody: AtpC | gamma subunit of ATP synthase, Immunogen: synthetic peptides derived from Arabidopsis thalina chloroplast localized ATP synthase subunit gamma chain 1 and 2 protein sequence ( At4g046 100
AS10 1604 Antibody: AtpF | CF0I subunit of ATP synthase , Immunogen: isolated CF0I subunit of the chloroplast ATP synthase complex , Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis thaliana, Spinaci 100 ul
AS09 312P Antibody: AtpC | gamma subunit of ATP synthase | blocking peptide, Immunogen: synthetic peptides derived from Arabidopsis thalina chloroplast localized ATP synthase subunit gamma chain 1and 2 protein 100
10-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 0.05 mg
10-288-22197F Vacuolar ATP synthase subunit G 1 - EC 3.6.3.14; V-ATPase G subunit 1; Vacuolar proton pump G subunit 1; V-ATPase 13 kDa subunit 1; Vacuolar ATP synthase subunit M16 0.1 mg
A3070 PDX1 Primary Antibody, PDX1, Species: Human Synthetic peptide Source: Rabbit Polyclonal 50ug
EIAAB11775 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Homo sapiens,Human,Mannose-P-dolichol synthase,MPD synthase
EIAAB38426 Homo sapiens,Human,N-acetylneuraminate synthase,N-acetylneuraminate-9-phosphate synthase,N-acetylneuraminic acid phosphate synthase,N-acetylneuraminic acid synthase,NANS,SAS,Sialic acid synthase
EIAAB11774 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,Dpm1,Mannose-P-dolichol synthase,Mouse,MPD synthase,Mus musculus


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur