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

Sucrose synthase 1 (AtSUS1) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 1)

 SUS1_ARATH              Reviewed;         808 AA.
P49040; B9DFM1; Q56WF2;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 3.
25-APR-2018, entry version 126.
RecName: Full=Sucrose synthase 1;
Short=AtSUS1;
EC=2.4.1.13;
AltName: Full=Sucrose-UDP glucosyltransferase 1;
Name=SUS1; OrderedLocusNames=At5g20830; ORFNames=T1M15.230;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. C24;
PubMed=8220487; DOI=10.1046/j.1365-313X.1993.04020367.x;
Martin T., Frommer W.B., Salanoubat M., Willmitzer L.;
"Expression of an Arabidopsis sucrose synthase gene indicates a role
in metabolization of sucrose both during phloem loading and in sink
organs.";
Plant J. 4:367-377(1993).
[2]
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).
[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=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-808.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
PubMed=10567234; DOI=10.1042/bj3440503;
Dejardin A., Sokolov L.N., Kleczkowski L.A.;
"Sugar/osmoticum levels modulate differential abscisic acid-
independent expression of two stress-responsive sucrose synthase genes
in Arabidopsis.";
Biochem. J. 344:503-509(1999).
[7]
GENE FAMILY, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=14739263; DOI=10.1093/jxb/erh047;
Baud S., Vaultier M.N., Rochat C.;
"Structure and expression profile of the sucrose synthase multigene
family in Arabidopsis.";
J. Exp. Bot. 55:397-409(2004).
[8]
BIOTECHNOLOGY.
PubMed=17499718; DOI=10.1016/j.febslet.2007.04.074;
Masada S., Kawase Y., Nagatoshi M., Oguchi Y., Terasaka K.,
Mizukami H.;
"An efficient chemoenzymatic production of small molecule glucosides
with in situ UDP-glucose recycling.";
FEBS Lett. 581:2562-2566(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[10]
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION, AND
DISRUPTION PHENOTYPE.
PubMed=17257168; DOI=10.1111/j.1365-313X.2006.03011.x;
Bieniawska Z., Paul Barratt D.H., Garlick A.P., Thole V., Kruger N.J.,
Martin C., Zrenner R., Smith A.M.;
"Analysis of the sucrose synthase gene family in Arabidopsis.";
Plant J. 49:810-828(2007).
[11]
TISSUE SPECIFICITY.
PubMed=18635527; DOI=10.1093/jxb/ern180;
Fallahi H., Scofield G.N., Badger M.R., Chow W.S., Furbank R.T.,
Ruan Y.L.;
"Localization of sucrose synthase in developing seed and siliques of
Arabidopsis thaliana reveals diverse roles for SUS during
development.";
J. Exp. Bot. 59:3283-3295(2008).
[12]
INDUCTION BY NUC.
PubMed=21265895; DOI=10.1111/j.1365-313X.2010.04432.x;
Seo P.J., Ryu J., Kang S.K., Park C.M.;
"Modulation of sugar metabolism by an INDETERMINATE DOMAIN
transcription factor contributes to photoperiodic flowering in
Arabidopsis.";
Plant J. 65:418-429(2011).
[13]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22184213; DOI=10.1073/pnas.1117099109;
Baroja-Fernandez E., Munoz F.J., Li J., Bahaji A., Almagro G.,
Montero M., Etxeberria E., Hidalgo M., Sesma M.T., Pozueta-Romero J.;
"Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis
mutant is sufficient to support normal cellulose and starch
production.";
Proc. Natl. Acad. Sci. U.S.A. 109:321-326(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
SUBUNIT, AND FUNCTION.
PubMed=21865170; DOI=10.1074/jbc.M111.275974;
Zheng Y., Anderson S., Zhang Y., Garavito R.M.;
"The structure of sucrose synthase-1 from Arabidopsis thaliana and its
functional implications.";
J. Biol. Chem. 286:36108-36118(2011).
-!- FUNCTION: Sucrose-cleaving enzyme that provides UDP-glucose and
fructose for various metabolic pathways.
{ECO:0000269|PubMed:21865170}.
-!- CATALYTIC ACTIVITY: NDP-glucose + D-fructose = NDP + sucrose.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.37 mM for D-fructose (synthetic reaction) at pH 9.4
{ECO:0000269|PubMed:17257168};
KM=0.04 mM for UDP-glucose (synthetic reaction) at pH 9.4
{ECO:0000269|PubMed:17257168};
KM=31.58 mM for sucrose (degradative reaction) at pH 6
{ECO:0000269|PubMed:17257168};
KM=53 mM for sucrose (degradative reaction) at pH 7
{ECO:0000269|PubMed:22184213};
KM=0.08 mM for UDP (degradative reaction) at pH 6
{ECO:0000269|PubMed:17257168};
KM=0.39 mM for UDP (degradative reaction) at pH 7
{ECO:0000269|PubMed:22184213};
KM=0.17 mM for ADP (degradative reaction) at pH 7
{ECO:0000269|PubMed:22184213};
Vmax=11.14 umol/min/mg enzyme for synthetic reaction at pH 9.4
{ECO:0000269|PubMed:17257168};
Vmax=4.68 umol/min/mg enzyme for degradative reaction at pH 6
{ECO:0000269|PubMed:17257168};
Vmax=585 umol/min/mg enzyme for degradative reaction at pH 7
{ECO:0000269|PubMed:22184213};
pH dependence:
Optimum pH is 6.0-7.0 for degradative reaction (PubMed:22184213,
PubMed:17257168). Optimum pH is 7.0 for synthetic reaction
(PubMed:22184213). Optimum pH is 9.0-9.5 for synthetic reaction
(PubMed:17257168). {ECO:0000269|PubMed:17257168,
ECO:0000269|PubMed:22184213};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21865170}.
-!- TISSUE SPECIFICITY: Expressed in the phloem of leaves and in
roots. Detected in the whole plant but more precisely confined to
the vasculature in cotyledons, mature leaves and siliques.
{ECO:0000269|PubMed:14739263, ECO:0000269|PubMed:17257168,
ECO:0000269|PubMed:18635527, ECO:0000269|PubMed:8220487}.
-!- INDUCTION: By cold, drought and anaerobic stress. By sugar or
osmoticum. By anoxia in the roots (at protein level). Up-regulated
by NUC/IDD8. {ECO:0000269|PubMed:10567234,
ECO:0000269|PubMed:14739263, ECO:0000269|PubMed:17257168,
ECO:0000269|PubMed:21265895, ECO:0000269|PubMed:8220487}.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:17257168}.
-!- BIOTECHNOLOGY: A one-pot system for efficient enzymatic production
of a wide range of glucosides couples the activities of two
recombinant enzymes, UDP-glucose: curcumin glucosyltransferase
from Catharanthus roseus (CaUGT2) and sucrose synthase from
Arabidopsis thaliana (AtSUS1). UDP, a product inhibitor of UDP-
glucosyltransferase, was removed from the system and used for
regeneration of UDP-glucose by the second enzyme, AtSUS1. The
productivity was increased several-fold and UDP-glucose initially
added to the reaction mixture could be reduced to one-tenth of the
normal level. {ECO:0000269|PubMed:17499718}.
-!- SIMILARITY: Belongs to the glycosyltransferase 1 family. Plant
sucrose synthase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD94975.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; X70990; CAA50317.1; -; Genomic_DNA.
EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92894.1; -; Genomic_DNA.
EMBL; CP002688; AED92895.1; -; Genomic_DNA.
EMBL; CP002688; ANM71045.1; -; Genomic_DNA.
EMBL; AK316826; BAH19538.1; -; mRNA.
EMBL; AK222090; BAD94975.1; ALT_INIT; mRNA.
RefSeq; NP_001031915.1; NM_001036838.2.
RefSeq; NP_001332603.1; NM_001343687.1.
RefSeq; NP_197583.1; NM_122090.4.
UniGene; At.21918; -.
PDB; 3S27; X-ray; 2.91 A; A/B/C/D/E/F/G/H=1-808.
PDB; 3S28; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-808.
PDB; 3S29; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-808.
PDBsum; 3S27; -.
PDBsum; 3S28; -.
PDBsum; 3S29; -.
ProteinModelPortal; P49040; -.
SMR; P49040; -.
BioGrid; 17481; 4.
STRING; 3702.AT5G20830.1; -.
CAZy; GT4; Glycosyltransferase Family 4.
iPTMnet; P49040; -.
SwissPalm; P49040; -.
PaxDb; P49040; -.
PRIDE; P49040; -.
EnsemblPlants; AT5G20830.1; AT5G20830.1; AT5G20830.
EnsemblPlants; AT5G20830.2; AT5G20830.2; AT5G20830.
EnsemblPlants; AT5G20830.3; AT5G20830.3; AT5G20830.
GeneID; 832206; -.
Gramene; AT5G20830.1; AT5G20830.1; AT5G20830.
Gramene; AT5G20830.2; AT5G20830.2; AT5G20830.
Gramene; AT5G20830.3; AT5G20830.3; AT5G20830.
KEGG; ath:AT5G20830; -.
Araport; AT5G20830; -.
TAIR; locus:2180489; AT5G20830.
eggNOG; KOG0853; Eukaryota.
eggNOG; COG0438; LUCA.
HOGENOM; HOG000240125; -.
InParanoid; P49040; -.
KO; K00695; -.
OMA; DVENKEH; -.
OrthoDB; EOG0936023J; -.
PhylomeDB; P49040; -.
BioCyc; ARA:AT5G20830-MONOMER; -.
BioCyc; MetaCyc:AT5G20830-MONOMER; -.
BRENDA; 2.4.1.13; 399.
EvolutionaryTrace; P49040; -.
PRO; PR:P49040; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P49040; baseline and differential.
Genevisible; P49040; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0016157; F:sucrose synthase activity; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0009413; P:response to flooding; IEP:TAIR.
GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
GO; GO:0010555; P:response to mannitol; IEP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
GO; GO:0072708; P:response to sorbitol; IEP:UniProtKB.
GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
GO; GO:0005985; P:sucrose metabolic process; IEA:InterPro.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR000368; Sucrose_synth.
InterPro; IPR012820; Sucrose_synthase_pln/cyn.
Pfam; PF00534; Glycos_transf_1; 1.
Pfam; PF00862; Sucrose_synth; 1.
TIGRFAMs; TIGR02470; sucr_synth; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycosyltransferase;
Reference proteome; Stress response; Transferase.
CHAIN 1 808 Sucrose synthase 1.
/FTId=PRO_0000204644.
REGION 277 754 GT-B glycosyltransferase.
CONFLICT 61 61 R -> Q (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 108 108 V -> L (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 222 222 S -> P (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 405 405 N -> D (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 434 434 C -> QC (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 609 609 V -> I (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 751 752 EK -> DE (in Ref. 1; CAA50317).
{ECO:0000305}.
CONFLICT 799 800 Missing (in Ref. 1; CAA50317).
{ECO:0000305}.
HELIX 16 18 {ECO:0000244|PDB:3S29}.
TURN 19 23 {ECO:0000244|PDB:3S29}.
HELIX 30 40 {ECO:0000244|PDB:3S28}.
STRAND 43 47 {ECO:0000244|PDB:3S28}.
HELIX 48 53 {ECO:0000244|PDB:3S28}.
TURN 54 58 {ECO:0000244|PDB:3S28}.
HELIX 61 63 {ECO:0000244|PDB:3S28}.
TURN 64 68 {ECO:0000244|PDB:3S29}.
HELIX 69 74 {ECO:0000244|PDB:3S28}.
STRAND 76 81 {ECO:0000244|PDB:3S28}.
STRAND 83 93 {ECO:0000244|PDB:3S28}.
STRAND 96 103 {ECO:0000244|PDB:3S28}.
STRAND 109 112 {ECO:0000244|PDB:3S28}.
HELIX 114 126 {ECO:0000244|PDB:3S28}.
STRAND 136 138 {ECO:0000244|PDB:3S28}.
HELIX 140 143 {ECO:0000244|PDB:3S28}.
HELIX 152 154 {ECO:0000244|PDB:3S28}.
HELIX 158 169 {ECO:0000244|PDB:3S28}.
TURN 170 172 {ECO:0000244|PDB:3S28}.
HELIX 174 186 {ECO:0000244|PDB:3S28}.
STRAND 192 196 {ECO:0000244|PDB:3S28}.
HELIX 203 219 {ECO:0000244|PDB:3S28}.
HELIX 226 235 {ECO:0000244|PDB:3S28}.
HELIX 246 261 {ECO:0000244|PDB:3S28}.
HELIX 265 274 {ECO:0000244|PDB:3S28}.
STRAND 280 284 {ECO:0000244|PDB:3S28}.
STRAND 292 294 {ECO:0000244|PDB:3S28}.
HELIX 303 325 {ECO:0000244|PDB:3S28}.
STRAND 333 339 {ECO:0000244|PDB:3S28}.
STRAND 346 348 {ECO:0000244|PDB:3S27}.
STRAND 351 355 {ECO:0000244|PDB:3S28}.
STRAND 360 367 {ECO:0000244|PDB:3S28}.
STRAND 369 371 {ECO:0000244|PDB:3S28}.
STRAND 374 376 {ECO:0000244|PDB:3S28}.
TURN 382 384 {ECO:0000244|PDB:3S28}.
HELIX 386 388 {ECO:0000244|PDB:3S28}.
HELIX 389 403 {ECO:0000244|PDB:3S28}.
STRAND 409 414 {ECO:0000244|PDB:3S28}.
HELIX 415 429 {ECO:0000244|PDB:3S28}.
STRAND 433 436 {ECO:0000244|PDB:3S28}.
HELIX 441 444 {ECO:0000244|PDB:3S28}.
TURN 446 451 {ECO:0000244|PDB:3S28}.
HELIX 452 459 {ECO:0000244|PDB:3S28}.
HELIX 461 474 {ECO:0000244|PDB:3S28}.
STRAND 475 481 {ECO:0000244|PDB:3S28}.
HELIX 483 487 {ECO:0000244|PDB:3S28}.
STRAND 490 492 {ECO:0000244|PDB:3S28}.
HELIX 497 499 {ECO:0000244|PDB:3S28}.
STRAND 500 504 {ECO:0000244|PDB:3S28}.
TURN 505 507 {ECO:0000244|PDB:3S28}.
STRAND 508 513 {ECO:0000244|PDB:3S28}.
STRAND 521 523 {ECO:0000244|PDB:3S28}.
TURN 530 532 {ECO:0000244|PDB:3S28}.
TURN 539 541 {ECO:0000244|PDB:3S28}.
HELIX 544 546 {ECO:0000244|PDB:3S28}.
HELIX 547 555 {ECO:0000244|PDB:3S28}.
STRAND 563 565 {ECO:0000244|PDB:3S28}.
STRAND 570 572 {ECO:0000244|PDB:3S27}.
STRAND 574 578 {ECO:0000244|PDB:3S28}.
TURN 583 586 {ECO:0000244|PDB:3S28}.
HELIX 587 596 {ECO:0000244|PDB:3S28}.
HELIX 598 603 {ECO:0000244|PDB:3S28}.
STRAND 605 609 {ECO:0000244|PDB:3S28}.
HELIX 620 635 {ECO:0000244|PDB:3S28}.
STRAND 639 645 {ECO:0000244|PDB:3S28}.
HELIX 651 663 {ECO:0000244|PDB:3S28}.
STRAND 667 670 {ECO:0000244|PDB:3S28}.
STRAND 675 677 {ECO:0000244|PDB:3S28}.
HELIX 679 686 {ECO:0000244|PDB:3S28}.
STRAND 691 697 {ECO:0000244|PDB:3S28}.
HELIX 699 702 {ECO:0000244|PDB:3S28}.
TURN 705 707 {ECO:0000244|PDB:3S28}.
STRAND 710 712 {ECO:0000244|PDB:3S28}.
HELIX 717 733 {ECO:0000244|PDB:3S28}.
HELIX 736 751 {ECO:0000244|PDB:3S28}.
HELIX 755 776 {ECO:0000244|PDB:3S28}.
TURN 777 779 {ECO:0000244|PDB:3S28}.
HELIX 780 793 {ECO:0000244|PDB:3S28}.
HELIX 795 801 {ECO:0000244|PDB:3S28}.
SEQUENCE 808 AA; 92998 MW; CDB56C6A57BD852E CRC64;
MANAERMITR VHSQRERLNE TLVSERNEVL ALLSRVEAKG KGILQQNQII AEFEALPEQT
RKKLEGGPFF DLLKSTQEAI VLPPWVALAV RPRPGVWEYL RVNLHALVVE ELQPAEFLHF
KEELVDGVKN GNFTLELDFE PFNASIPRPT LHKYIGNGVD FLNRHLSAKL FHDKESLLPL
LKFLRLHSHQ GKNLMLSEKI QNLNTLQHTL RKAEEYLAEL KSETLYEEFE AKFEEIGLER
GWGDNAERVL DMIRLLLDLL EAPDPCTLET FLGRVPMVFN VVILSPHGYF AQDNVLGYPD
TGGQVVYILD QVRALEIEML QRIKQQGLNI KPRILILTRL LPDAVGTTCG ERLERVYDSE
YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TYTEDAAVEL SKELNGKPDL IIGNYSDGNL
VASLLAHKLG VTQCTIAHAL EKTKYPDSDI YWKKLDDKYH FSCQFTADIF AMNHTDFIIT
STFQEIAGSK ETVGQYESHT AFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFPYTEEK
RRLTKFHSEI EELLYSDVEN KEHLCVLKDK KKPILFTMAR LDRVKNLSGL VEWYGKNTRL
RELANLVVVG GDRRKESKDN EEKAEMKKMY DLIEEYKLNG QFRWISSQMD RVRNGELYRY
ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCKGGPA EIIVHGKSGF HIDPYHGDQA
ADTLADFFTK CKEDPSHWDE ISKGGLQRIE EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR
LEARRYLEMF YALKYRPLAQ AVPLAQDD


Related products :

Catalog number Product name Quantity
ISTOC1010 Calibration Kit;Blank, 0.25mg_L C NIST Sucrose, 0.5mg_L C NIST Sucrose,0.75mg_L C NIST Sucrose Kit
ISTOC1167 Calibration Kit;Blank, 0.25mg_L C NIST Sucrose,0.5mg_L C NIST Sucrose,0.75mg_L C NIST Sucrose. Kit
ISTOC1167 Calibration Kit;Blank, 0.25mg L C NIST Sucrose,0.5mg L C NIST Sucrose,0.75mg L C NIST Sucrose. Kit
ISTOC1010 Calibration Kit;Blank, 0.25mg L C NIST Sucrose, 0.5mg L C NIST Sucrose,0.75mg L C NIST Sucrose Kit
B295 Phenol Red Sucrose Broth USE : For Sucrose fermentation studies of microorganisms. 5x500gm
B295 Phenol Red Sucrose Broth USE For Sucrose fermentation studies of microorganisms. Qty per Litre of Medium: 21
B294 Phenol Red Sucrose Agar USE For Sucrose fermentation studies of microorganisms Qty per Litre of Medium: 41
B294 Phenol Red Sucrose Agar USE : For Sucrose fermentation studies of microorganisms 5x500gm
ISTOC1080 System Suitability USP Set;2 x H2O,0.5mg L C Sucrose,0.5mg L C,C6H4O2,0.25mg L C NIST Sucrose 60ml
ESUC-100 EnzyChrom™ Sucrose Assay Kit, Quantitative determination of sucrose by colorimetric (565nm) method. 100Tests
LSP04-1LT Media,Linsmaier & Skoog with Buffer and Sucrose,with macro- and micronutrients, vitamins, and 30 g_L sucrose; pH buffered to 5.7 +_-0.2 1L
LSP04-10LT Media,Linsmaier & Skoog with Buffer and Sucrose,with macro- and micronutrients, vitamins, and 30 g_L sucrose; pH buffered to 5.7 +_-0.3 10L
LSP04-50LT Media,Linsmaier & Skoog with Buffer and Sucrose,with macro- and micronutrients, vitamins, and 30 g_L sucrose; pH buffered to 5.7 +_-0.4 50L
25339-99-5 Sucrose monolaurate Sucrose laurate 1g
ESUC-100 EnzyChrom™ Sucrose Assay Kit, Quantitative determination of sucrose by colorimetric (565nm) method. Procedure 70 min. Kit size 100 tests. Detection limit 17 µM. Shelf life 3 months. Shipping on i 100tests
31835-02-6 Sucrose (Z,Z)-9,12-octadecadienoate Sucrose (Z,Z)-9,12-oct 1g
ISTOC1080 System Suitability USP Set;2 x H2O,0.5mg_L C Sucrose,0.5mg_L C,C6H4O2,0.25mg_L C NIST Sucrose 60ml
ISTOC1050 Calibration Kit; 2 x calibration blanks, 0.25mg_L C Sucrose and 0.5mg_L Sucrose. 500ml Bottles Kit
AS11 1796 Antibody: Sucrose synthase 4 , Immunogen: recombinant part ofPopulus trichocarpaSucrose synthase 4 B9MWW3, Host: rabbit, polyclonal, Confirmed reactivity: to be determined 100
20312482-1 Sucrose synthase 4 (rabbit) 100 ug
AS06 185 Sucrose Phosphate Synthase (SPS) 0.1 ml
AS06185 Sucrose phosphate synthase _ SPS 0.1 ml
AS06 185 Sucrose Phosphate Synthase (SPS) 0.1 ml
AS03035A Sucrose phosphate synthase _ SPS 0.2 mg
ISTOC1050 Calibration Kit; 2 x calibration blanks, 0.25mg L C Sucrose and 0.5mg L Sucrose. 500ml Bottles Kit


 

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