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Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Acyl-CoA synthetase 1) (ACS1) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain acyl-CoA synthetase 2) (LACS 2) (Long-chain fatty acid-CoA ligase 2) (Palmitoyl-CoA ligase 1) (Palmitoyl-CoA ligase 2)

 ACSL1_HUMAN             Reviewed;         698 AA.
P33121; B7Z452; D3DP57; P41215; Q8N8V7; Q8TA99;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
23-MAY-2018, entry version 172.
RecName: Full=Long-chain-fatty-acid--CoA ligase 1;
EC=6.2.1.3;
AltName: Full=Acyl-CoA synthetase 1;
Short=ACS1;
AltName: Full=Long-chain acyl-CoA synthetase 1;
Short=LACS 1;
AltName: Full=Long-chain acyl-CoA synthetase 2;
Short=LACS 2;
AltName: Full=Long-chain fatty acid-CoA ligase 2;
AltName: Full=Palmitoyl-CoA ligase 1;
AltName: Full=Palmitoyl-CoA ligase 2;
Name=ACSL1; Synonyms=FACL1, FACL2, LACS, LACS1, LACS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=1607358; DOI=10.1093/oxfordjournals.jbchem.a123707;
Abe T., Fujino T., Fukuyama R., Minoshima S., Shimizu N., Toh H.,
Suzuki H., Yamamoto T.;
"Human long-chain acyl-CoA synthetase: structure and chromosomal
location.";
J. Biochem. 111:123-128(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8584017; DOI=10.1007/BF01076899;
Ghosh B., Barbosa E., Singh I.;
"Molecular cloning and sequencing of human palmitoyl-CoA ligase and
its tissue specific expression.";
Mol. Cell. Biochem. 151:77-81(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 395-698 (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-8; 12-19; 341-349; 377-386; 562-572; 633-640 AND
655-675, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[8]
TISSUE SPECIFICITY.
PubMed=10548543; DOI=10.1042/bj3440135;
Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.;
"Identification and molecular characterization of acyl-CoA synthetase
in human red cells and erythroid precursor.";
Biochem. J. 344:135-143(1999).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Activation of long-chain fatty acids for both synthesis
of cellular lipids, and degradation via beta-oxidation.
Preferentially uses palmitoleate, oleate and linoleate.
-!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
diphosphate + an acyl-CoA.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
Single-pass type III membrane protein {ECO:0000250}. Peroxisome
membrane {ECO:0000250}; Single-pass type III membrane protein
{ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type
III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type III membrane protein
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P33121-1; Sequence=Displayed;
Name=2;
IsoId=P33121-2; Sequence=VSP_009604;
Note=May be due to a competing acceptor splice site. No
experimental confirmation available.;
Name=3;
IsoId=P33121-3; Sequence=VSP_054391;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in liver, heart, skeletal
muscle, kidney and erythroid cells, and to a lesser extent in
brain, lung, placenta and pancreas. {ECO:0000269|PubMed:10548543}.
-!- DEVELOPMENTAL STAGE: Expressed during the early stages of
erythroid development while expression is very low in
reticulocytes and young erythrocytes.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC04704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D10040; BAA00931.1; -; mRNA.
EMBL; L09229; AAB00959.1; -; mRNA.
EMBL; AK096117; BAC04704.1; ALT_INIT; mRNA.
EMBL; AK296826; BAH12438.1; -; mRNA.
EMBL; AC079257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04662.1; -; Genomic_DNA.
EMBL; CH471056; EAX04663.1; -; Genomic_DNA.
EMBL; CH471056; EAX04665.1; -; Genomic_DNA.
EMBL; BC026290; AAH26290.1; -; mRNA.
EMBL; BC050073; AAH50073.1; -; mRNA.
CCDS; CCDS3839.1; -. [P33121-1]
CCDS; CCDS68826.1; -. [P33121-3]
PIR; JX0202; JX0202.
RefSeq; NP_001273637.1; NM_001286708.1. [P33121-1]
RefSeq; NP_001273639.1; NM_001286710.1. [P33121-3]
RefSeq; NP_001273640.1; NM_001286711.1.
RefSeq; NP_001273641.1; NM_001286712.1.
RefSeq; NP_001986.2; NM_001995.3. [P33121-1]
RefSeq; XP_005262885.1; XM_005262828.1. [P33121-1]
RefSeq; XP_005262886.1; XM_005262829.1. [P33121-1]
RefSeq; XP_005262888.1; XM_005262831.1. [P33121-1]
RefSeq; XP_011530044.1; XM_011531742.1. [P33121-1]
RefSeq; XP_016863376.1; XM_017007887.1. [P33121-1]
RefSeq; XP_016863377.1; XM_017007888.1. [P33121-3]
RefSeq; XP_016863378.1; XM_017007889.1. [P33121-3]
UniGene; Hs.406678; -.
ProteinModelPortal; P33121; -.
SMR; P33121; -.
BioGrid; 108476; 13.
IntAct; P33121; 2.
STRING; 9606.ENSP00000281455; -.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB00171; Adenosine triphosphate.
SwissLipids; SLP:000000199; -.
SwissLipids; SLP:000001468; -. [P33121-1]
iPTMnet; P33121; -.
PhosphoSitePlus; P33121; -.
SwissPalm; P33121; -.
BioMuta; ACSL1; -.
DMDM; 417241; -.
EPD; P33121; -.
MaxQB; P33121; -.
PaxDb; P33121; -.
PeptideAtlas; P33121; -.
PRIDE; P33121; -.
Ensembl; ENST00000281455; ENSP00000281455; ENSG00000151726. [P33121-1]
Ensembl; ENST00000504342; ENSP00000425006; ENSG00000151726. [P33121-1]
Ensembl; ENST00000513317; ENSP00000426150; ENSG00000151726. [P33121-3]
Ensembl; ENST00000515030; ENSP00000422607; ENSG00000151726. [P33121-1]
GeneID; 2180; -.
KEGG; hsa:2180; -.
UCSC; uc003iwt.2; human. [P33121-1]
CTD; 2180; -.
DisGeNET; 2180; -.
EuPathDB; HostDB:ENSG00000151726.13; -.
GeneCards; ACSL1; -.
HGNC; HGNC:3569; ACSL1.
HPA; HPA011316; -.
HPA; HPA011964; -.
MIM; 152425; gene.
neXtProt; NX_P33121; -.
OpenTargets; ENSG00000151726; -.
PharmGKB; PA27966; -.
eggNOG; KOG1256; Eukaryota.
eggNOG; COG1022; LUCA.
GeneTree; ENSGT00690000101725; -.
HOGENOM; HOG000159459; -.
HOVERGEN; HBG050452; -.
InParanoid; P33121; -.
KO; K01897; -.
OMA; ECVMLCH; -.
OrthoDB; EOG091G03G9; -.
PhylomeDB; P33121; -.
TreeFam; TF313877; -.
BioCyc; MetaCyc:HS07766-MONOMER; -.
BRENDA; 6.2.1.3; 2681.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
SIGNOR; P33121; -.
ChiTaRS; ACSL1; human.
GeneWiki; ACSL1; -.
GenomeRNAi; 2180; -.
PRO; PR:P33121; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000151726; -.
CleanEx; HS_ACSL1; -.
ExpressionAtlas; P33121; baseline and differential.
Genevisible; P33121; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum;
Fatty acid metabolism; Glycoprotein; Ligase; Lipid metabolism;
Magnesium; Membrane; Microsome; Mitochondrion;
Mitochondrion outer membrane; Nitration; Nucleotide-binding;
Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 698 Long-chain-fatty-acid--CoA ligase 1.
/FTId=PRO_0000193104.
TRANSMEM 25 45 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 46 698 Cytoplasmic. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.7}.
MOD_RES 9 9 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P18163}.
MOD_RES 84 84 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18163}.
MOD_RES 207 207 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 356 356 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 386 386 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41216}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 632 632 N6-acetyllysine.
{ECO:0000250|UniProtKB:P18163}.
CARBOHYD 135 135 O-linked (GlcNAc) serine. {ECO:0000250}.
VAR_SEQ 306 331 NTVNPCPDDTLISFLPLAHMFERVVE -> KALPLSASDTH
ISYLPLAHIYEQLLK (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054391.
VAR_SEQ 508 517 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_009604.
CONFLICT 21 23 YVR -> CV (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 37 38 AA -> SRR (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 44 47 YATR -> RPRH (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 55 56 CD -> WH (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 229 229 A -> S (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 385 385 L -> V (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 400 401 EL -> DV (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 477 477 A -> T (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 492 494 VDV -> GWQL (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 502 502 A -> S (in Ref. 2; AAB00959).
{ECO:0000305}.
CONFLICT 695 695 T -> I (in Ref. 2; AAB00959).
{ECO:0000305}.
SEQUENCE 698 AA; 77943 MW; FD6669453589D362 CRC64;
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR
CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL LMDDLKVLQP
TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE LRSGIIRNNS LWDRLIFHKV
QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV
GAPMPCNLIK LVDVEEMNYM AAEGEGEVCV KGPNVFQGYL KDPAKTAEAL DKDGWLHTGD
IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI
VVPDVETLCS WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF EQVKGITLHP
ELFSIDNGLL TPTMKAKRPE LRNYFRSQID DLYSTIKV


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EIAAB36851 Acsvl1,Facvl1,Fatp2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Long-chain-fatty-acid--CoA ligase,Mouse,Mus musculus,Slc27a2,Solute carrier family 27 member 2
EIAAB36850 Acsvl1,Facvl1,Fatp2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Long-chain-fatty-acid--CoA ligase,Rat,Rattus norvegicus,Slc27a2,Solute carrier family 27 membe
EIAAB36852 ACSVL1,FACVL1,FATP2,FATP-2,Fatty acid transport protein 2,Fatty-acid-coenzyme A ligase, very long-chain 1,Homo sapiens,Human,Long-chain-fatty-acid--CoA ligase,SLC27A2,Solute carrier family 27 member 2
EIAAB12849 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,hELO2,Homo sapiens,Human,LCE,Long-chain fatty-acyl elongas
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
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
EIAAB36860 ACSVL2,FACVL2,FATP1,FATP-6,Fatty acid transport protein 6,Fatty-acid-coenzyme A ligase, very long-chain 2,Homo sapiens,Human,hVLCS-H1,Long-chain fatty acid transport protein 6,SLC27A6,Solute carrier f
EIAAB36854 ACSVL3,FATP3,FATP-3,Fatty acid transport protein 3,Homo sapiens,Human,Long-chain fatty acid transport protein 3,PSEC0067,SLC27A3,Solute carrier family 27 member 3,UNQ367_PRO703,Very long-chain acyl-Co
EIAAB36859 Acsb,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,Fatp5,FATP-5,Fatty acid transport protein 5,Rat,Rattus norvegicus,Slc27a5,Solute carrier family 27 member
EIAAB36857 Acsb,Acsvl6,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,Fatp5,FATP-5,Fatty acid transport protein 5,Mouse,Mus musculus,Slc27a5,Solute carrier family 27 mem
E1090m Rat ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 3 96T
CSB-EL001193RA Rat Long-chain-fatty-acid--CoA ligase 4(ACSL4) ELISA kit 96T
CSB-EP300208EKN Recombinant Ba(E.coli-k12) Long-chain-fatty-acid--CoA ligase 500ug
E10511h Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 1 96T
E1437r Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 5 96T
E10451r Rat ELISA Kit FOR Long-chain-fatty-acid--CoA ligase ACSBG2 96T
E1477r Mouse ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 4 96T
E14531h Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 3 96T
CSB-EL001194RA Rat Long-chain-fatty-acid--CoA ligase 5(ACSL5) ELISA kit 96T
E1061Rb Human ELISA Kit FOR Long-chain-fatty-acid--CoA ligase 6 96T
CSB-EL001195RA Rat Long-chain-fatty-acid--CoA ligase 6(ACSL6) ELISA kit 96T
CSB-EL001192RA Rat Long-chain-fatty-acid--CoA ligase 3(ACSL3) ELISA kit 96T
CSB-EL001192RA Rat Long-chain-fatty-acid--CoA ligase 3(ACSL3) ELISA kit SpeciesRat 96T


 

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