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Acid beta-fructofuranosidase 4, vacuolar (At beta fruct4) (AtBETAFRUCT4) (EC 3.2.1.26) (Acid invertase 4) (AI 4) (Acid sucrose hydrolase 4) (Vacuolar invertase 4) (Inv-V4) (VAC-INV 4) (VI 4)

 INVA4_ARATH             Reviewed;         664 AA.
Q39041; Q7DLW9; Q8GX36;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=Acid beta-fructofuranosidase 4, vacuolar {ECO:0000303|PubMed:9332372};
Short=At beta fruct4 {ECO:0000303|PubMed:9332372};
Short=AtBETAFRUCT4 {ECO:0000303|PubMed:9332372};
EC=3.2.1.26 {ECO:0000255|PROSITE-ProRule:PRU10067};
AltName: Full=Acid invertase 4 {ECO:0000303|PubMed:9332372};
Short=AI 4 {ECO:0000303|PubMed:9332372};
AltName: Full=Acid sucrose hydrolase 4 {ECO:0000305};
AltName: Full=Vacuolar invertase 4 {ECO:0000303|PubMed:14871666};
Short=Inv-V4 {ECO:0000303|PubMed:14871666};
Short=VAC-INV 4 {ECO:0000303|PubMed:16481625};
Short=VI 4 {ECO:0000303|PubMed:14871666};
Flags: Precursor;
Name=BFRUCT4 {ECO:0000303|PubMed:9332372};
Synonyms=BETAFRUCT4 {ECO:0000303|PubMed:9332372};
OrderedLocusNames=At1g12240 {ECO:0000312|Araport:AT1G12240};
ORFNames=T28K15.3 {ECO:0000312|EMBL:AAG12569.1};
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=9332372; DOI=10.1016/S0378-1119(97)00268-0;
Haouazine-Takvorian N., Tymowska-Lalanne Z., Takvorian A., Tregear J.,
Lejeune B., Lecharny A., Kreis M.;
"Characterization of two members of the Arabidopsis thaliana gene
family, At beta fruct3 and At beta fruct4, coding for vacuolar
invertases.";
Gene 197:239-251(1997).
[2]
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).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-636.
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[6]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=12773619; DOI=10.1073/pnas.1230987100;
Rojo E., Zouhar J., Carter C., Kovaleva V., Raikhel N.V.;
"A unique mechanism for protein processing and degradation in
Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 100:7389-7394(2003).
[7]
ENZYME REGULATION.
PubMed=14871666; DOI=10.1016/j.bbapap.2003.09.017;
Rausch T., Greiner S.;
"Plant protein inhibitors of invertases.";
Biochim. Biophys. Acta 1696:253-261(2004).
[8]
DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
STRAIN=cv. Landsberg erecta;
PubMed=15056893; DOI=10.1271/bbb.68.602;
Mitsuhashi W., Sasaki S., Kanazawa A., Yang Y.-Y., Kamiya Y.,
Toyomasu T.;
"Differential expression of acid invertase genes during seed
germination in Arabidopsis thaliana.";
Biosci. Biotechnol. Biochem. 68:602-608(2004).
[9]
INDUCTION BY VIRULENT P.SYRINGAE.
PubMed=16807755; DOI=10.1007/s00425-006-0303-3;
Bonfig K.B., Schreiber U., Gabler A., Roitsch T., Berger S.;
"Infection with virulent and avirulent P. syringae strains
differentially affects photosynthesis and sink metabolism in
Arabidopsis leaves.";
Planta 225:1-12(2006).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=16481625; DOI=10.1073/pnas.0511015103;
Sergeeva L.I., Keurentjes J.J., Bentsink L., Vonk J.,
van der Plas L.H.W., Koornneef M., Vreugdenhil D.;
"Vacuolar invertase regulates elongation of Arabidopsis thaliana roots
as revealed by QTL and mutant analysis.";
Proc. Natl. Acad. Sci. U.S.A. 103:2994-2999(2006).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=20207708; DOI=10.1104/pp.110.154443;
Naegele T., Henkel S., Hoermiller I., Sauter T., Sawodny O.,
Ederer M., Heyer A.G.;
"Mathematical modeling of the central carbohydrate metabolism in
Arabidopsis reveals a substantial regulatory influence of vacuolar
invertase on whole plant carbon metabolism.";
Plant Physiol. 153:260-272(2010).
[12]
SUBCELLULAR LOCATION, MUTAGENESIS OF 7-LEU-LEU-8; 9-PRO-ILE-10;
14-GLU--GLU-16; 18-LEU--TYR-21 AND 21-TYR--LEU-24, AND DOMAIN.
STRAIN=cv. Columbia;
PubMed=21899678; DOI=10.1111/j.1600-0854.2011.01276.x;
Jung C., Lee G.J., Jang M., Lee M., Lee J., Kang H., Sohn E.J.,
Hwang I.;
"Identification of sorting motifs of AtbetaFruct4 for trafficking from
the ER to the vacuole through the Golgi and PVC.";
Traffic 12:1774-1792(2011).
[13]
SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-2; 3-SER-SER-4; SER-3; SER-4;
ASP-5; ALA-6; 7-LEU-LEU-8; LEU-7; LEU-8; PRO-9; ILE-10; SER-11; ALA-12
AND 21-TYR--LEU-24, AND DOMAIN.
PubMed=23737500; DOI=10.1093/pcp/pct075;
Xiang L., Van den Ende W.;
"Trafficking of plant vacuolar invertases: from a membrane-anchored to
a soluble status. Understanding sorting information in their complex
N-terminal motifs.";
Plant Cell Physiol. 54:1263-1277(2013).
-!- FUNCTION: Possible role in the continued mobilization of sucrose
to sink organs (PubMed:20207708). Regulates root elongation
(PubMed:16481625). {ECO:0000269|PubMed:16481625,
ECO:0000269|PubMed:20207708}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
fructofuranoside residues in beta-D-fructofuranosides.
{ECO:0000255|PROSITE-ProRule:PRU10067}.
-!- ENZYME REGULATION: Inhibited by C/VIF1 and C/VIF2.
{ECO:0000269|PubMed:14871666}.
-!- PATHWAY: Glycan biosynthesis; sucrose metabolism. {ECO:0000305}.
-!- SUBUNIT: May be present in two forms, a 70 kDa monomer and a
heterodimer of the 30 kDa and 38 kDa subunits. The ratio of the
levels of the two forms within cells appears to be regulated
developmentally (By similarity). {ECO:0000250|UniProtKB:P29001}.
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:12773619}.
Endoplasmic reticulum membrane {ECO:0000269|PubMed:21899678,
ECO:0000269|PubMed:23737500}; Single-pass type II membrane
protein. Golgi apparatus membrane {ECO:0000269|PubMed:21899678,
ECO:0000269|PubMed:23737500}; Single-pass type II membrane
protein. Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:21899678}; Single-pass type II membrane
protein. Prevacuolar compartment membrane
{ECO:0000269|PubMed:21899678}; Single-pass type II membrane
protein. Vacuole membrane {ECO:0000269|PubMed:21899678}; Single-
pass type II membrane protein. Vacuole lumen
{ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}.
Note=Located in the lytic vacuole but not in the protein storage
vacuole. Remains inserted into membranes on its way to the lytic
vacuole, following the classical sorting pathway from the
endoplasmic reticulum. Released into the lumen of the vacuole from
the tonoplast through a proteolytic processing.
{ECO:0000269|PubMed:21899678, ECO:0000269|PubMed:23737500}.
-!- TISSUE SPECIFICITY: Mostly expressed in stems, roots and flowers,
and, to a lower extent, in mature leaves.
{ECO:0000269|PubMed:9332372}.
-!- DEVELOPMENTAL STAGE: Expressed during germination et seedling
growth. {ECO:0000269|PubMed:15056893}.
-!- INDUCTION: Induced by gibberellin (e.g. gibberellic acid GA) that
accumulates in seeds after red light treatment (PubMed:15056893).
Accumulates upon infection with virulent but not with avirulent
P.syringae (PubMed:16807755). Degraded in a VPEgamma-dependent
manner during senescence (PubMed:12773619).
{ECO:0000269|PubMed:12773619, ECO:0000269|PubMed:15056893,
ECO:0000269|PubMed:16807755}.
-!- DOMAIN: The LCPYTRL domain (18-24) is critical for trafficking
from the trans-Golgi network to the prevacuolar compartment and
from the prevacuolar compartment to the central vacuole
(PubMed:21899678). The PRRRRP domain (36-41) is involved in
sorting to the vacuole (PubMed:23737500). At least two Arg are
needed for correct delivery and the presence of two neighboring
Pro seems to contribute to the sorting efficiency
(PubMed:23737500). {ECO:0000269|PubMed:21899678,
ECO:0000269|PubMed:23737500}.
-!- DISRUPTION PHENOTYPE: Reduced carbon fixation rates during the
day, but increased respiration during the night (PubMed:20207708).
Shorter roots (PubMed:16481625). {ECO:0000269|PubMed:16481625,
ECO:0000269|PubMed:20207708}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC43067.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X97749; CAA66330.1; -; mRNA.
EMBL; Y11559; CAA72321.1; -; Genomic_DNA.
EMBL; AC022522; AAG12569.1; -; Genomic_DNA.
EMBL; CP002684; AEE28855.1; -; Genomic_DNA.
EMBL; AY046009; AAK76683.1; -; mRNA.
EMBL; AY142666; AAN13204.1; -; mRNA.
EMBL; AK118459; BAC43067.1; ALT_INIT; mRNA.
PIR; E86257; E86257.
PIR; S71276; S71276.
RefSeq; NP_563901.1; NM_101096.3.
UniGene; At.24440; -.
ProteinModelPortal; Q39041; -.
SMR; Q39041; -.
BioGrid; 23017; 2.
IntAct; Q39041; 2.
STRING; 3702.AT1G12240.1; -.
CAZy; GH32; Glycoside Hydrolase Family 32.
iPTMnet; Q39041; -.
PaxDb; Q39041; -.
PRIDE; Q39041; -.
EnsemblPlants; AT1G12240.1; AT1G12240.1; AT1G12240.
GeneID; 837777; -.
Gramene; AT1G12240.1; AT1G12240.1; AT1G12240.
KEGG; ath:AT1G12240; -.
Araport; AT1G12240; -.
TAIR; locus:2201966; AT1G12240.
eggNOG; KOG0228; Eukaryota.
eggNOG; COG1621; LUCA.
HOGENOM; HOG000181427; -.
InParanoid; Q39041; -.
KO; K01193; -.
OMA; FFCQDEL; -.
OrthoDB; EOG093605WU; -.
PhylomeDB; Q39041; -.
BioCyc; ARA:AT1G12240-MONOMER; -.
UniPathway; UPA00238; -.
PRO; PR:Q39041; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q39041; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0004564; F:beta-fructofuranosidase activity; ISS:TAIR.
GO; GO:0004575; F:sucrose alpha-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0071370; P:cellular response to gibberellin stimulus; IEP:UniProtKB.
GO; GO:0080022; P:primary root development; IMP:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 2.115.10.20; -; 1.
InterPro; IPR021792; Beta-fructofuranosidase.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001362; Glyco_hydro_32.
InterPro; IPR018053; Glyco_hydro_32_AS.
InterPro; IPR013189; Glyco_hydro_32_C.
InterPro; IPR013148; Glyco_hydro_32_N.
InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
Pfam; PF11837; DUF3357; 1.
Pfam; PF08244; Glyco_hydro_32C; 1.
Pfam; PF00251; Glyco_hydro_32N; 1.
SMART; SM00640; Glyco_32; 1.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF75005; SSF75005; 1.
PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
1: Evidence at protein level;
Abscisic acid signaling pathway; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Glycosidase; Golgi apparatus;
Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix; Vacuole; Zymogen.
PROPEP 1 108 Removed in mature form.
{ECO:0000250|UniProtKB:P80065}.
/FTId=PRO_0000417019.
CHAIN 109 664 Acid beta-fructofuranosidase 4, vacuolar.
/FTId=PRO_0000417020.
TOPO_DOM 1 43 Cytoplasmic. {ECO:0000305}.
TRANSMEM 44 64 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 65 664 Lumenal. {ECO:0000305}.
REGION 132 135 Substrate binding.
{ECO:0000250|UniProtKB:Q43866}.
REGION 194 195 Substrate binding.
{ECO:0000250|UniProtKB:Q43866}.
REGION 258 259 Substrate binding.
{ECO:0000250|UniProtKB:Q43866}.
MOTIF 7 8 Critical for endoplasmic reticulum
export. {ECO:0000269|PubMed:21899678}.
MOTIF 9 10 Critical for endoplasmic reticulum
export. {ECO:0000269|PubMed:21899678}.
MOTIF 14 16 Critical for trafficking from the trans-
Golgi network to the prevacuolar
compartment and from the prevacuolar
compartment to the central vacuole.
{ECO:0000269|PubMed:21899678}.
ACT_SITE 135 135 {ECO:0000255|PROSITE-ProRule:PRU10067}.
BINDING 151 151 Substrate.
{ECO:0000250|UniProtKB:Q43866}.
BINDING 159 159 Substrate.
{ECO:0000250|UniProtKB:Q43866}.
BINDING 313 313 Substrate.
{ECO:0000250|UniProtKB:Q43866}.
BINDING 346 346 Substrate.
{ECO:0000250|UniProtKB:Q43866}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 510 558 {ECO:0000250|UniProtKB:Q43866}.
MUTAGEN 2 2 Missing: No effect on localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 3 4 Missing: Endoplasmic reticulum
localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 3 3 Missing: Partial retention in the
endoplasmic reticulum.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 4 4 Missing: Partial retention in the
endoplasmic reticulum.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 5 5 Missing: Endoplasmic reticulum
localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 6 6 Missing: No effect on localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 7 8 LL->AA: Reduced vacuolar trafficking.
{ECO:0000269|PubMed:21899678}.
MUTAGEN 7 8 Missing: Endoplasmic reticulum
localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 7 7 Missing: Partial retention in the
endoplasmic reticulum.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 8 8 Missing: Partial retention in the
endoplasmic reticulum.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 9 10 PI->AA: Reduced vacuolar trafficking.
{ECO:0000269|PubMed:21899678}.
MUTAGEN 9 9 P->A: Partial retention in the
endoplasmic reticulum.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 10 10 Missing: Endoplasmic reticulum
localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 11 11 Missing: Endoplasmic reticulum
localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 12 12 Missing: No effect on localization.
{ECO:0000269|PubMed:23737500}.
MUTAGEN 14 16 EEE->AAA: Reduced vacuolar trafficking.
{ECO:0000269|PubMed:21899678}.
MUTAGEN 18 21 LCPY->AAAA: Reduced vacuolar trafficking.
{ECO:0000269|PubMed:21899678}.
MUTAGEN 21 24 YTRL->AAAA: Reduced vacuolar trafficking.
{ECO:0000269|PubMed:21899678}.
MUTAGEN 21 24 Missing: No effect on localization.
{ECO:0000269|PubMed:23737500}.
SEQUENCE 664 AA; 73844 MW; 85948869AEDABD8B CRC64;
MASSDALLPI SAREEEPLCP YTRLPMADPN QETHGPRRRR PFKGLLAVSF GLLFIAFYVA
LIATHDGSRS NDEGIDETET ITSRARLAGV SEKRNDGLWK LSGDRNTPAF EWNNSMLSWQ
RTAFHFQPEQ NWMNDPNGPL FYKGWYHFFY QYNPNAAVWG DIVWGHAVSR DLIHWVHLPI
AMVADQWYDS NGVWTGSATF LPDGSIVMLY TGSTDKAVQV QNLAYPEDPN DPLLLKWVKF
PGNPVLVPPP GILPKDFRDP TTAWKTSEGK WRITIGSKLN KTGISLVYDT IDFKTYEKLD
TLLHRVPNTG MWECVDFYPV SKTAGNGLDT SVNGPDVKHI VKASMDDTRF DHYAVGTYFD
SNGTWIPDDP TIDVGMTASL RYDYGKFYAS KSFYDQNKGR RVLWSWIGES DSEASDVQKG
WSSLQGIPRT VVLDTKTGKN LVQWPVEEIK SLRLSSKQFD LEVGPGSVVP VDVGSAAQLD
IEAEFEINKE SLDKIIGNAS VVAEAEEFSC EKSGGSTVRG ALGPFGFSVL ATESLSEQTP
VYFYVAKGKD SELKTFFCTD TSRSSVANDV VKPIYGSVVP VLKGEKLTMR ILVDHSIVEA
FGQGGRTCIT SRVYPTTAIY GAAKLFLFNN ALDATVTASF TVWQMNSAFI HPYSDEAVRA
LSRT


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EIAAB11627 Deoxyribonuclease II beta,Deoxyribonuclease-2-beta,DLAD,DNase II beta,DNase II-like acid DNase,DNASE2B,DNase2-like acid DNase,Endonuclease DLAD,Homo sapiens,Human
E1022Ge ELISA kit 3-hydroxybutyric acid,beta-hydroxybutyrate,beta-Hydroxybutyric acid,BHA 96T
U1022Ge CLIA 3-hydroxybutyric acid,beta-hydroxybutyrate,beta-Hydroxybutyric acid,BHA 96T
E1022Ge ELISA 3-hydroxybutyric acid,beta-hydroxybutyrate,beta-Hydroxybutyric acid,BHA 96T
EIAAB11628 Deoxyribonuclease II beta,Deoxyribonuclease-2-beta,Dlad,DNase II beta,DNase II-like acid DNase,Dnase2b,DNase2-like acid DNase,Endonuclease DLAD,Mouse,Mus musculus
EIAAB11626 Deoxyribonuclease II beta,Deoxyribonuclease-2-beta,Dlad,DNase II beta,DNase II-like acid DNase,Dnase2b,DNase2-like acid DNase,Endonuclease DLAD,Rat,Rattus norvegicus
EIAAB45907 ATP6N1,ATP6N1A,ATP6V0A1,Clathrin-coated vesicle_synaptic vesicle proton pump 116 kDa subunit,Homo sapiens,Human,Vacuolar adenosine triphosphatase subunit Ac116,Vacuolar proton pump subunit 1,Vacuolar
EIAAB45906 Atp6n1,Atp6v0a1,Clathrin-coated vesicle_synaptic vesicle proton pump 116 kDa subunit,Rat,Rattus norvegicus,Vacuolar adenosine triphosphatase subunit Ac116,Vacuolar proton pump subunit 1,Vacuolar proto
32142-31-7 Vanillic acid 4-beta-D-glucoside Vanillic acid 4-beta-D-gl 1g
orb82682 Human Defensin beta 1 (47) protein Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. Recombinant Human BD-1 is a 5.0 kDa protein containing 47 amino acid residues. Fo 1 mg
H-1775.0025 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 25.0 mg
H-1775.0025 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 25.0 mg
H-1775.0005 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 5.0 mg
H-1775.0005 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 5.0 mg
EIAAB45904 Atp6n1,Atp6v0a1,Clathrin-coated vesicle_synaptic vesicle proton pump 116 kDa subunit,Mouse,Mus musculus,Vacuolar adenosine triphosphatase subunit Ac116,Vacuolar proton pump subunit 1,Vacuolar proton t
EIAAB45908 ATP6N1,ATP6V0A1,Bos taurus,Bovine,Clathrin-coated vesicle_synaptic vesicle proton pump 116 kDa subunit,Vacuolar adenosine triphosphatase subunit Ac116,Vacuolar proton pump subunit 1,Vacuolar proton tr
30-973 ETFB is the electron-transfer-flavoprotein, beta polypeptide, which shuttles electrons between primary flavoprotein dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism and th 0.05 mg
2112-2 Acetic Acid (50 mM) Ethanoic acid, methanecarboxylic acid, ethylic acid 2 ml


 

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