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Fatty acid synthase 1, isoform A (EC 1.1.1.100) (EC 1.3.1.10) (EC 2.3.1.38) (EC 2.3.1.39) (EC 2.3.1.41) (EC 2.3.1.85) (EC 3.1.2.14) (EC 4.2.1.59)

 Q9VQL7_DROME            Unreviewed;      2438 AA.
Q9VQL7; Q9Y129;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 146.
SubName: Full=Fatty acid synthase 1, isoform A {ECO:0000313|EMBL:AAF51148.1};
EC=1.1.1.100 {ECO:0000313|EMBL:AAF51148.1};
EC=1.3.1.10 {ECO:0000313|EMBL:AAF51148.1};
EC=2.3.1.38 {ECO:0000313|EMBL:AAF51148.1};
EC=2.3.1.39 {ECO:0000313|EMBL:AAF51148.1};
EC=2.3.1.41 {ECO:0000313|EMBL:AAF51148.1};
EC=2.3.1.85 {ECO:0000313|EMBL:AAF51148.1};
EC=3.1.2.14 {ECO:0000313|EMBL:AAF51148.1};
EC=4.2.1.59 {ECO:0000313|EMBL:AAF51148.1};
Name=FASN1 {ECO:0000313|EMBL:AAF51148.1,
ECO:0000313|FlyBase:FBgn0283427};
Synonyms=anon-EST:Posey235 {ECO:0000313|EMBL:AAF51148.1},
anon-EST:Posey43 {ECO:0000313|EMBL:AAF51148.1},
anon-WO0138581.1 {ECO:0000313|EMBL:AAF51148.1},
BcDNA:GH07626 {ECO:0000313|EMBL:AAF51148.1},
BcDNA:gh07626 {ECO:0000313|EMBL:AAF51148.1},
dFAS {ECO:0000313|EMBL:AAF51148.1},
DM_7295848 {ECO:0000313|EMBL:AAF51148.1},
Dmel\CG3523 {ECO:0000313|EMBL:AAF51148.1},
FAS {ECO:0000313|EMBL:AAF51148.1}, Fas {ECO:0000313|EMBL:AAF51148.1},
fas {ECO:0000313|EMBL:AAF51148.1},
FAS[CG3523] {ECO:0000313|EMBL:AAF51148.1},
FASN {ECO:0000313|EMBL:AAF51148.1},
FASN[CG3523] {ECO:0000313|EMBL:AAF51148.1},
Fatty acid synthase {ECO:0000313|EMBL:AAF51148.1};
ORFNames=CG3523 {ECO:0000313|EMBL:AAF51148.1,
ECO:0000313|FlyBase:FBgn0283427},
Dmel_CG3523 {ECO:0000313|EMBL:AAF51148.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J.,
Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[3] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
[5] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[6] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[7] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[8] {ECO:0000313|EMBL:AAF51148.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
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EMBL; AE014134; AAF51148.1; -; Genomic_DNA.
RefSeq; NP_608748.1; NM_134904.3.
UniGene; Dm.7216; -.
ProteinModelPortal; Q9VQL7; -.
SMR; Q9VQL7; -.
IntAct; Q9VQL7; 3.
ESTHER; drome-CG3523; Thioesterase.
PRIDE; Q9VQL7; -.
EnsemblMetazoa; FBtr0077659; FBpp0077343; FBgn0283427.
GeneID; 33524; -.
UCSC; CG3523-RA; d. melanogaster.
CTD; 33524; -.
FlyBase; FBgn0283427; FASN1.
eggNOG; KOG1202; Eukaryota.
eggNOG; COG3321; LUCA.
GeneTree; ENSGT00530000063309; -.
OrthoDB; EOG091G003K; -.
Reactome; R-DME-163765; ChREBP activates metabolic gene expression.
Reactome; R-DME-199220; Vitamin B5 (pantothenate) metabolism.
Reactome; R-DME-75105; Fatty acyl-CoA biosynthesis.
ChiTaRS; FASN1; fly.
GenomeRNAi; 33524; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0027571; -.
ExpressionAtlas; Q9VQL7; differential.
Genevisible; Q9VQL7; DM.
GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:UniProtKB-EC.
GO; GO:0004312; F:fatty acid synthase activity; IDA:FlyBase.
GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:FlyBase.
GO; GO:0005977; P:glycogen metabolic process; IMP:FlyBase.
GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
GO; GO:0019432; P:triglyceride biosynthetic process; IMP:FlyBase.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 1.10.1470.20; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 1.
Gene3D; 3.40.50.1820; -; 2.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR013149; ADH_C.
InterPro; IPR023102; Fatty_acid_synthase_dom_2.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020843; PKS_ER.
InterPro; IPR013968; PKS_KR.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR001031; Thioesterase.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF00107; ADH_zinc_N; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08659; KR; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF00975; Thioesterase; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00826; PKS_DH; 1.
SMART; SM00829; PKS_ER; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 2.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF53901; SSF53901; 2.
SUPFAM; SSF55048; SSF55048; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
1: Evidence at protein level;
Acyltransferase {ECO:0000313|EMBL:AAF51148.1};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Hydrolase {ECO:0000313|EMBL:AAF51148.1};
Lyase {ECO:0000313|EMBL:AAF51148.1};
Oxidoreductase {ECO:0000313|EMBL:AAF51148.1};
Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258};
Proteomics identification {ECO:0000213|PeptideAtlas:Q9VQL7};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Transferase {ECO:0000313|EMBL:AAF51148.1}.
DOMAIN 2046 2123 Carrier. {ECO:0000259|PROSITE:PS50075}.
MOD_RES 2081 2081 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000256|PROSITE-ProRule:PRU00258}.
SEQUENCE 2438 AA; 266444 MW; D336104713119865 CRC64;
MPARFAEEVI TAEPAQRAAP QLDLGGGHYV PRQQHLNDEI AITGFSGRLP ESSTIEEFKQ
NLFDGVDMVN DDPRRWERGL YGLPDRIGKL KDSDLENFDQ QFFGVHQKQA ECMDPLLRML
LELTHEAIID AGLNPSDLRG SRTGVYIGVS NSETEQHWCS DADRVNGYGL TGCARAMFAN
RISFTFDFKG PSYSIDTACS SSLYALEQAF SDMREGKVDN ALVAGAGLIL KPTMSLQFKR
LNMLSPDGSC KAFDESGNGY VRSDGCVVLL LQRTSAARRV YASILNVRTN TDGFKEQGIT
YPIGKMQNRL IRETYEEIGL NPADVVYVEA HGTGTKVGDP QEVNSITDFF CKDRTTPLLI
GSVKSNMGHS EPASGVCSVA KILIAMEEGV IPGNLHYNKP NPDLYGLVDG RLKVVDRNLP
WNGGIIGLNS FGFGGANAHV ILKSNPKPKA LTPKDGALKV VLASGRTFEA VEQLLESAST
NADDDEYLQL INEIHSKAIP NHFFRGYGVV SSKGTHQREV IESNDDKRPI WYIYSGMGSQ
WASMAKDLMK IEAFAKTIQR CADVLKPEGV DLIDVLTRST DKSFENILNS FISIAAMQVA
LTDLLSSLGI HPDGIVGHSV GELGCAYADG CFTPEQTVLA AYWRGKSILD TQLAKGKMAA
VGLSWEDAHS RVPSDCFPVC HNSEDNCTIS GPEASIEALV AKLNAEGVFA KAVNSSGYAF
HSKYIAEAGP KLRKSLEKII PNAKNRTARW ISTSIPESAW NTPVAKQSSA AYHVNNLLSP
VLFHEALQHV PKNAISVEIA PHGLLQAILK RALGPDATNL SLVKRGHENN VEFFLTNVGK
LFAAGAQPQV LTLVRPISYP VGRGTPMLNS KVGWDHTQKW LVAKFGKETS SGETIVEVDL
SKEDDAFLAG HTIDGRILFP ATGYMTLAWQ TFAKMQGSEF HKTPVVMENL VFHRATILNK
NAVVKFGINF FDGTGAFEIC ESGSLAVSGK ITIPESIDNE ELPLEEQTPS AVAKELGTND
VYKELRLRGY DYGGIFRGIV RSDTVASTGK LQWVDNWISF MDTMLQFSIL SKNLRELYLP
TRIERAVINP AKHFELLSAL TKEEQVETGL PVQWYSDINV IKSAGVELRG LKANLAQRRP
GTQAPPTLER YQFVPNINTT DLNENSEKAR LHALDVAIQV IIENSSGAVK LKGVELANGR
NPDVLVANRL LQIIEGEPVL TGDVAVVTSN NNEETITAAL GDSGVRVVSK DVLKEPVEQN
CHFVFGIDVL SRPDTKTLEN SIASIRENGF LILEETLPTY TKTGRALLTK FGFVAVQEQS
LGATRVLVLA RKAVDLKTRK SVVVVATEQN FNWVDDLKAA LATAATEEQY VYVVCQGEEL
FGAVGLMTCI KNENGGKLAR LVFVQDAKAE KFSLTSTLYR QQLEKDLISN VLKNGAWGTF
RHLKLETQQA TLQVEHAYVN ALVKGDLASL KWIEAAQADT AATVDKNLET CTVYYAPINF
RDVMLTSGKL AADALPGDLA EQDCVLGLEF AGRDTQGRRV MAMVPAKSLA TTCVASKRMM
WQIPEKWTME EASTVPCVYS TVYYALVVRG QMKKGEKILI HAGSGGVGQA AISVALAHGL
TVFTTVGSKE KREFLLKRFP KLQERNIGNS RDTSFEQLVL RETKGRGVDL VLNSLSEEKL
QASIRCLGLN GRFLEIGKFD LSNNSPLGMS VFLKNTSFHG ILLDSVMEGE EEMQNQVVSL
VAEGIKTGAV VPLPTSVFND QQVEQAFRFM ASGKHIGKVV IKVRDEEAGK KALQPKPRLI
NAIPRTYMHP EKSYILVGGL GGFGLELTNW LVTRGARYIV LTSRSGVKTG YQGLMIRRWQ
ERGVKVVIDT SDVTTAAGAK KLLENSNKLA LVGGIFNLAA VLRDALIEDQ TAKDFKTVAD
PKVTATKYLD QFSRDICTEL DYFICFSSVS CGRGNIGQTN YGLANSAMER ICEQRQVSGF
PGTAIQWGAI GDTGLVLENL GDNDTVIGGT LPQRMPSCLQ TIDLFLQQPH PVVASMVVAE
KRKSDQSAGV SLIATIANIL GLRDTKNIQD GASLADLGMD SLMSAEIKQT LERNFDIVLS
AQEIRQLTFG ALKAMDGGAD VKPAAAAPAA AAGVPEANIT SGGSSRTASP MGDGTQVVFT
TSLIPTEAIV QLDTKAPANS KQSPIFFISP IEGFASALEP LAKRLEVPAY GLQYTEAVPS
DSLESAAKFF IKQLRTVQPK GPYKLAGYSF GCLLTYVMAG ILEETNEVAN VIMLDGAPSY
VNWYTSSFKQ RYTDGTNADN DNQSYGLAYF GIVLANIDYK ALVRLLIVIP TWEEKLERFA
ELMSNEITQP VETIKKSATL FYKKLELADG YQPTLKLKTN VTLVKPTDNS AKLDEDYRLK
EVCTKPVEVH TVEGNHRTFL IEDQSLKTIQ SILKRLFN


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FASN11-A Fatty acid synthase 0.1 mg
GTX30468 Fatty acid synthase 100 µl
NB400-114 Fatty acid synthase 0.1 ml
077-66A C75 Fatty Acid Synthase Inhibitor _ 5mg 5 mg
077-66 C75 Fatty Acid Synthase Inhibitor _ 1mg 1 mg
GTX110470 Fatty acid synthase 100 µg
GTX109833 Fatty acid synthase 100 µg
FASN12-A Fatty acid synthase 0.1 mg
26-772 Fatty acid amide hydrolases, such as FAAH1 and FAAH2, hydrolyze primary fatty acid amide substrates and may play a role in fatty acid catabolism.Fatty acid amide hydrolases, such as FAAH1 (FAAH; MIM 6 0.05 mg
30-857 Fatty acid amide hydrolases, such as FAAH1 and FAAH2, hydrolyze primary fatty acid amide substrates and may play a role in fatty acid catabolism.Fatty acid amide hydrolases, such as FAAH1 (FAAH; MIM 6 0.05 mg
EIAAB12848 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acyl-CoA elongase,Lce,Long chain fatty acid elongase,Masr,Mouse,Mus musculus,Myelin-associated SUR
YF-MA12964 anti-Fatty Acid Synthase (S1) 100 ug
YF-MA12965 anti-Fatty Acid Synthase (3A2) 100 ug
YF-PA11722 anti-Fatty Acid Synthase 50 ug


 

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