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Fatty acid synthase 1, isoform C (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)

 B7Z001_DROME            Unreviewed;      2540 AA.
B7Z001;
03-MAR-2009, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 2.
20-DEC-2017, entry version 82.
SubName: Full=Fatty acid synthase 1, isoform C {ECO:0000313|EMBL:ACL82985.2};
EC=1.1.1.100 {ECO:0000313|EMBL:ACL82985.2};
EC=1.3.1.10 {ECO:0000313|EMBL:ACL82985.2};
EC=2.3.1.38 {ECO:0000313|EMBL:ACL82985.2};
EC=2.3.1.39 {ECO:0000313|EMBL:ACL82985.2};
EC=2.3.1.41 {ECO:0000313|EMBL:ACL82985.2};
EC=2.3.1.85 {ECO:0000313|EMBL:ACL82985.2};
EC=3.1.2.14 {ECO:0000313|EMBL:ACL82985.2};
EC=4.2.1.59 {ECO:0000313|EMBL:ACL82985.2};
Name=FASN1 {ECO:0000313|EMBL:ACL82985.2,
ECO:0000313|FlyBase:FBgn0283427};
Synonyms=anon-EST:Posey235 {ECO:0000313|EMBL:ACL82985.2},
anon-EST:Posey43 {ECO:0000313|EMBL:ACL82985.2},
anon-WO0138581.1 {ECO:0000313|EMBL:ACL82985.2},
BcDNA:GH07626 {ECO:0000313|EMBL:ACL82985.2},
BcDNA:gh07626 {ECO:0000313|EMBL:ACL82985.2},
dFAS {ECO:0000313|EMBL:ACL82985.2},
DM_7295848 {ECO:0000313|EMBL:ACL82985.2},
Dmel\CG3523 {ECO:0000313|EMBL:ACL82985.2},
FAS {ECO:0000313|EMBL:ACL82985.2}, Fas {ECO:0000313|EMBL:ACL82985.2},
fas {ECO:0000313|EMBL:ACL82985.2},
FAS[CG3523] {ECO:0000313|EMBL:ACL82985.2},
FASN {ECO:0000313|EMBL:ACL82985.2},
FASN[CG3523] {ECO:0000313|EMBL:ACL82985.2},
Fatty acid synthase {ECO:0000313|EMBL:ACL82985.2};
ORFNames=CG3523 {ECO:0000313|EMBL:ACL82985.2,
ECO:0000313|FlyBase:FBgn0283427},
Dmel_CG3523 {ECO:0000313|EMBL:ACL82985.2};
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:ACL82985.2, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:ACL82985.2, 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:ACL82985.2, 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:ACL82985.2, 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:ACL82985.2, 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:RESEARCH0084.1-RESEARCH0084.20(2002).
[5] {ECO:0000313|EMBL:ACL82985.2, 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:ACL82985.2, 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:ACL82985.2, 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:ACL82985.2, 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; ACL82985.2; -; Genomic_DNA.
RefSeq; NP_001137778.2; NM_001144306.2.
UniGene; Dm.7216; -.
SMR; B7Z001; -.
STRING; 7227.FBpp0288532; -.
PaxDb; B7Z001; -.
PRIDE; B7Z001; -.
EnsemblMetazoa; FBtr0335387; FBpp0307371; FBgn0027571.
GeneID; 33524; -.
KEGG; dme:Dmel_CG3523; -.
CTD; 33524; -.
FlyBase; FBgn0283427; FASN1.
eggNOG; KOG1202; Eukaryota.
eggNOG; COG3321; LUCA.
GeneTree; ENSGT00530000063309; -.
InParanoid; B7Z001; -.
KO; K00665; -.
OMA; DVNKPKY; -.
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; CG3523; fly.
GenomeRNAi; 33524; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0027571; -.
ExpressionAtlas; B7Z001; differential.
Genevisible; B7Z001; DM.
GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
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; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR029058; AB_hydrolase.
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:ACL82985.2};
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Hydrolase {ECO:0000313|EMBL:ACL82985.2};
Lyase {ECO:0000313|EMBL:ACL82985.2};
Oxidoreductase {ECO:0000313|EMBL:ACL82985.2};
Proteomics identification {ECO:0000213|PeptideAtlas:B7Z001};
Reference proteome {ECO:0000313|Proteomes:UP000000803};
Transferase {ECO:0000313|EMBL:ACL82985.2}.
DOMAIN 2148 2225 Carrier. {ECO:0000259|PROSITE:PS50075}.
MOD_RES 2183 2183 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000256|PROSITE-ProRule:PRU00258}.
SEQUENCE 2540 AA; 278000 MW; C9CFC916C679637D CRC64;
MPLQLNLLQA VDQPHPVAFK PNNCSTHQPQ HSPSTQNNGK SARANRRRRR RRNKQQQNSQ
QPDAFRDTDA QLTPSTSSST PHSAPNDRQD HLNSQFNPES INMPARFAEE VITAEPAQRA
APQLDLGGGH YVPRQQHLND EIAITGFSGR LPESSTIEEF KQNLFDGVDM VNDDPRRWER
GLYGLPDRIG KLKDSDLENF DQQFFGVHQK QAECMDPLLR MLLELTHEAI IDAGLNPSDL
RGSRTGVYIG VSNSETEQHW CSDADRVNGY GLTGCARAMF ANRISFTFDF KGPSYSIDTA
CSSSLYALEQ AFSDMREGKV DNALVAGAGL ILKPTMSLQF KRLNMLSPDG SCKAFDESGN
GYVRSDGCVV LLLQRTSAAR RVYASILNVR TNTDGFKEQG ITYPIGKMQN RLIRETYEEI
GLNPADVVYV EAHGTGTKVG DPQEVNSITD FFCKDRTTPL LIGSVKSNMG HSEPASGVCS
VAKILIAMEE GVIPGNLHYN KPNPDLYGLV DGRLKVVDRN LPWNGGIIGL NSFGFGGANA
HVILKSNPKP KALTPKDGAL KVVLASGRTF EAVEQLLESA STNADDDEYL QLINEIHSKA
IPNHFFRGYG VVSSKGTHQR EVIESNDDKR PIWYIYSGMG SQWASMAKDL MKIEAFAKTI
QRCADVLKPE GVDLIDVLTR STDKSFENIL NSFISIAAMQ VALTDLLSSL GIHPDGIVGH
SVGELGCAYA DGCFTPEQTV LAAYWRGKSI LDTQLAKGKM AAVGLSWEDA HSRVPSDCFP
VCHNSEDNCT ISGPEASIEA LVAKLNAEGV FAKAVNSSGY AFHSKYIAEA GPKLRKSLEK
IIPNAKNRTA RWISTSIPES AWNTPVAKQS SAAYHVNNLL SPVLFHEALQ HVPKNAISVE
IAPHGLLQAI LKRALGPDAT NLSLVKRGHE NNVEFFLTNV GKLFAAGAQP QVLTLVRPIS
YPVGRGTPML NSKVGWDHTQ KWLVAKFGKE TSSGETIVEV DLSKEDDAFL AGHTIDGRIL
FPATGYMTLA WQTFAKMQGS EFHKTPVVME NLVFHRATIL NKNAVVKFGI NFFDGTGAFE
ICESGSLAVS GKITIPESID NEELPLEEQT PSAVAKELGT NDVYKELRLR GYDYGGIFRG
IVRSDTVAST GKLQWVDNWI SFMDTMLQFS ILSKNLRELY LPTRIERAVI NPAKHFELLS
ALTKEEQVET GLPVQWYSDI NVIKSAGVEL RGLKANLAQR RPGTQAPPTL ERYQFVPNIN
TTDLNENSEK ARLHALDVAI QVIIENSSGA VKLKGVELAN GRNPDVLVAN RLLQIIEGEP
VLTGDVAVVT SNNNEETITA ALGDSGVRVV SKDVLKEPVE QNCHFVFGID VLSRPDTKTL
ENSIASIREN GFLILEETLP TYTKTGRALL TKFGFVAVQE QSLGATRVLV LARKAVDLKT
RKSVVVVATE QNFNWVDDLK AALATAATEE QYVYVVCQGE ELFGAVGLMT CIKNENGGKL
ARLVFVQDAK AEKFSLTSTL YRQQLEKDLI SNVLKNGAWG TFRHLKLETQ QATLQVEHAY
VNALVKGDLA SLKWIEAAQA DTAATVDKNL ETCTVYYAPI NFRDVMLTSG KLAADALPGD
LAEQDCVLGL EFAGRDTQGR RVMAMVPAKS LATTCVASKR MMWQIPEKWT MEEASTVPCV
YSTVYYALVV RGQMKKGEKI LIHAGSGGVG QAAISVALAH GLTVFTTVGS KEKREFLLKR
FPKLQERNIG NSRDTSFEQL VLRETKGRGV DLVLNSLSEE KLQASIRCLG LNGRFLEIGK
FDLSNNSPLG MSVFLKNTSF HGILLDSVME GEEEMQNQVV SLVAEGIKTG AVVPLPTSVF
NDQQVEQAFR FMASGKHIGK VVIKVRDEEA GKKALQPKPR LINAIPRTYM HPEKSYILVG
GLGGFGLELT NWLVTRGARY IVLTSRSGVK TGYQGLMIRR WQERGVKVVI DTSDVTTAAG
AKKLLENSNK LALVGGIFNL AAVLRDALIE DQTAKDFKTV ADPKVTATKY LDQFSRDICT
ELDYFICFSS VSCGRGNIGQ TNYGLANSAM ERICEQRQVS GFPGTAIQWG AIGDTGLVLE
NLGDNDTVIG GTLPQRMPSC LQTIDLFLQQ PHPVVASMVV AEKRKSDQSA GVSLIATIAN
ILGLRDTKNI QDGASLADLG MDSLMSAEIK QTLERNFDIV LSAQEIRQLT FGALKAMDGG
ADVKPAAAAP AAAAGVPEAN ITSGGSSRTA SPMGDGTQVV FTTSLIPTEA IVQLDTKAPA
NSKQSPIFFI SPIEGFASAL EPLAKRLEVP AYGLQYTEAV PSDSLESAAK FFIKQLRTVQ
PKGPYKLAGY SFGCLLTYVM AGILEETNEV ANVIMLDGAP SYVNWYTSSF KQRYTDGTNA
DNDNQSYGLA YFGIVLANID YKALVRLLIV IPTWEEKLER FAELMSNEIT QPVETIKKSA
TLFYKKLELA DGYQPTLKLK TNVTLVKPTD NSAKLDEDYR LKEVCTKPVE VHTVEGNHRT
FLIEDQSLKT IQSILKRLFN


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EIAAB12846 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acid elongase 2,Fatty acyl-CoA elongase,Lce,Long-chain fatty-acyl elongase,Rat,Rattus norvegicus,r
GTX30468 Fatty acid synthase 100 µl
AP14097PU-N Fatty acid synthase 0.1 mg
FASN12-A Fatty acid synthase 0.1 mg
FASN11-A Fatty acid synthase 0.1 mg
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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