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

Bile acyl-CoA synthetase (BACS) (EC 6.2.1.7) (Bile acid-CoA ligase) (BA-CoA ligase) (BAL) (Cholate--CoA ligase) (Fatty acid transport protein 5) (FATP-5) (Fatty-acid-coenzyme A ligase, very long-chain 3) (Solute carrier family 27 member 5) (Very long-chain acyl-CoA synthetase homolog 2) (VLCS-H2) (VLCSH2) (Very long-chain acyl-CoA synthetase-related protein) (VLACS-related) (VLACSR)

 S27A5_HUMAN             Reviewed;         690 AA.
Q9Y2P5; B3KVP6; B4DPQ1;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Bile acyl-CoA synthetase;
Short=BACS;
EC=6.2.1.7;
AltName: Full=Bile acid-CoA ligase;
Short=BA-CoA ligase;
Short=BAL;
AltName: Full=Cholate--CoA ligase;
AltName: Full=Fatty acid transport protein 5;
Short=FATP-5;
AltName: Full=Fatty-acid-coenzyme A ligase, very long-chain 3;
AltName: Full=Solute carrier family 27 member 5;
AltName: Full=Very long-chain acyl-CoA synthetase homolog 2;
Short=VLCS-H2;
Short=VLCSH2;
AltName: Full=Very long-chain acyl-CoA synthetase-related protein;
Short=VLACS-related;
Short=VLACSR;
Name=SLC27A5; Synonyms=ACSB, ACSVL6, FACVL3, FATP5;
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 SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=10479480; DOI=10.1006/mgme.1999.2883;
Steinberg S.J., Wang S.J., McGuinness M.C., Watkins P.A.;
"Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA
cloning and characterization of a second enzymatically active
protein.";
Mol. Genet. Metab. 68:32-42(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10749848; DOI=10.1074/jbc.C000015200;
Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.;
"The human liver-specific homolog of very long-chain acyl-CoA
synthetase is cholate:CoA ligase.";
J. Biol. Chem. 275:15605-15608(2000).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND TOPOLOGY.
PubMed=11980911; DOI=10.1074/jbc.M203295200;
Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G.,
Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D.,
Watkins P.A.;
"Participation of two members of the very long-chain acyl-CoA
synthetase family in bile acid synthesis and recycling.";
J. Biol. Chem. 277:24771-24779(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, 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).
-!- FUNCTION: Acyl-CoA synthetase involved in bile acid metabolism.
Proposed to catalyze the first step in the conjugation of C24 bile
acids (choloneates) to glycine and taurine before excretion into
bile canaliculi by activating them to their CoA thioesters. Seems
to activate secondary bile acids entering the liver from the
enterohepatic circulation. In vitro, also activates 3-alpha,7-
alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27
precursor of cholic acid deriving from the de novo synthesis from
cholesterol. {ECO:0000269|PubMed:10749848,
ECO:0000269|PubMed:11980911}.
-!- CATALYTIC ACTIVITY: ATP + cholate + CoA = AMP + diphosphate +
choloyl-CoA.
-!- CATALYTIC ACTIVITY: ATP + (25R)-3-alpha,7-alpha,12-alpha-
trihydroxy-5-beta-cholestan-26-oate + CoA = AMP + diphosphate +
(25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10479480}; Multi-pass membrane protein
{ECO:0000269|PubMed:10479480}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y2P5-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y2P5-2; Sequence=VSP_055810;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver.
{ECO:0000269|PubMed:10479480}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {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; AF064255; AAD29444.1; -; mRNA.
EMBL; AK123036; BAG53858.1; -; mRNA.
EMBL; AK298446; BAG60663.1; -; mRNA.
EMBL; AC012313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW72601.1; -; Genomic_DNA.
CCDS; CCDS12983.1; -. [Q9Y2P5-1]
CCDS; CCDS82415.1; -. [Q9Y2P5-2]
RefSeq; NP_001308125.1; NM_001321196.1. [Q9Y2P5-2]
RefSeq; NP_036386.1; NM_012254.2. [Q9Y2P5-1]
UniGene; Hs.292177; -.
ProteinModelPortal; Q9Y2P5; -.
SMR; Q9Y2P5; -.
BioGrid; 116191; 1.
IntAct; Q9Y2P5; 1.
STRING; 9606.ENSP00000263093; -.
ChEMBL; CHEMBL5196; -.
SwissLipids; SLP:000000429; -.
SwissLipids; SLP:000001315; -. [Q9Y2P5-1]
TCDB; 4.C.1.1.13; the fatty acid transporter (fat) family.
iPTMnet; Q9Y2P5; -.
PhosphoSitePlus; Q9Y2P5; -.
BioMuta; SLC27A5; -.
DMDM; 74739456; -.
PaxDb; Q9Y2P5; -.
PeptideAtlas; Q9Y2P5; -.
PRIDE; Q9Y2P5; -.
ProteomicsDB; 85854; -.
DNASU; 10998; -.
Ensembl; ENST00000263093; ENSP00000263093; ENSG00000083807. [Q9Y2P5-1]
Ensembl; ENST00000601355; ENSP00000470368; ENSG00000083807. [Q9Y2P5-2]
GeneID; 10998; -.
KEGG; hsa:10998; -.
UCSC; uc002qtc.3; human. [Q9Y2P5-1]
CTD; 10998; -.
DisGeNET; 10998; -.
EuPathDB; HostDB:ENSG00000083807.9; -.
GeneCards; SLC27A5; -.
HGNC; HGNC:10999; SLC27A5.
HPA; CAB056160; -.
HPA; CAB068239; -.
HPA; HPA007292; -.
MalaCards; SLC27A5; -.
MIM; 603314; gene.
neXtProt; NX_Q9Y2P5; -.
OpenTargets; ENSG00000083807; -.
PharmGKB; PA35873; -.
eggNOG; KOG1179; Eukaryota.
eggNOG; ENOG410XQ8T; LUCA.
GeneTree; ENSGT00550000074420; -.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; Q9Y2P5; -.
KO; K08748; -.
OMA; DCRQHGV; -.
OrthoDB; EOG091G0B76; -.
PhylomeDB; Q9Y2P5; -.
TreeFam; TF313430; -.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
ChiTaRS; SLC27A5; human.
GeneWiki; SLC27A5; -.
GenomeRNAi; 10998; -.
PRO; PR:Q9Y2P5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000083807; Expressed in 154 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_SLC27A5; -.
ExpressionAtlas; Q9Y2P5; baseline and differential.
Genevisible; Q9Y2P5; HS.
GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047747; F:cholate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0015245; F:fatty acid transmembrane transporter activity; IEA:Ensembl.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; TAS:Reactome.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
GO; GO:0046951; P:ketone body biosynthetic process; IEA:Ensembl.
GO; GO:0015911; P:plasma membrane long-chain fatty acid transport; IEA:Ensembl.
GO; GO:0006642; P:triglyceride mobilization; IEA:Ensembl.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR030302; FATP5.
PANTHER; PTHR43107:SF4; PTHR43107:SF4; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Endoplasmic reticulum; Fatty acid metabolism; Ligase;
Lipid metabolism; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 690 Bile acyl-CoA synthetase.
/FTId=PRO_0000193213.
TOPO_DOM 1 30 Cytoplasmic.
{ECO:0000305|PubMed:11980911}.
TRANSMEM 31 51 Helical. {ECO:0000255}.
TRANSMEM 56 76 Helical. {ECO:0000255}.
TOPO_DOM 77 690 Cytoplasmic.
{ECO:0000305|PubMed:11980911}.
NP_BIND 292 303 AMP. {ECO:0000255}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 146 229 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055810.
VARIANT 50 50 M -> T (in dbSNP:rs35350976).
/FTId=VAR_048243.
VARIANT 53 53 R -> W (in dbSNP:rs34415062).
/FTId=VAR_048244.
SEQUENCE 690 AA; 75385 MW; 011313424D794546 CRC64;
MGVRQQLALL LLLLLLLWGL GQPVWPVAVA LTLRWLLGDP TCCVLLGLAM LARPWLGPWV
PHGLSLAAAA LALTLLPARL PPGLRWLPAD VIFLAKILHL GLKIRGCLSR QPPDTFVDAF
ERRARAQPGR ALLVWTGPGA GSVTFGELDA RACQAAWALK AELGDPASLC AGEPTALLVL
ASQAVPALCM WLGLAKLGCP TAWINPHGRG MPLAHSVLSS GARVLVVDPD LRESLEEILP
KLQAENIRCF YLSHTSPTPG VGALGAALDA APSHPVPADL RAGITWRSPA LFIYTSGTTG
LPKPAILTHE RVLQMSKMLS LSGATADDVV YTVLPLYHVM GLVVGILGCL DLGATCVLAP
KFSTSCFWDD CRQHGVTVIL YVGELLRYLC NIPQQPEDRT HTVRLAMGNG LRADVWETFQ
QRFGPIRIWE VYGSTEGNMG LVNYVGRCGA LGKMSCLLRM LSPFELVQFD MEAAEPVRDN
QGFCIPVGLG EPGLLLTKVV SQQPFVGYRG PRELSERKLV RNVRQSGDVY YNTGDVLAMD
REGFLYFRDR LGDTFRWKGE NVSTHEVEGV LSQVDFLQQV NVYGVCVPGC EGKVGMAAVQ
LAPGQTFDGE KLYQHVRAWL PAYATPHFIR IQDAMEVTST FKLMKTRLVR EGFNVGIVVD
PLFVLDNRAQ SFRPLTAEMY QAVCEGTWRL


Related products :

Catalog number Product name Quantity
EIAAB36858 ACSB,ACSVL6,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,FACVL3,FATP5,FATP-5,Fatty acid transport protein 5,Fatty-acid-coenzyme A ligase, very long-chain 3,
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
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
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
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
18-003-42285 Long-chain-fatty-acid--CoA ligase 1 - EC 6.2.1.3; Long-chain acyl-CoA synthetase 1; LACS 1; Palmitoyl-CoA ligase 1; Long-chain fatty acid CoA ligase 2; Long-chain acyl-CoA synthetase 2; LACS 2; Acyl-C 0.05 mg Aff Pur
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
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
EIAAB36846 Fatp,Fatp1,FATP-1,Fatty acid transport protein 1,Long-chain fatty acid transport protein 1,Rat,Rattus norvegicus,Slc27a1,Solute carrier family 27 member 1
EIAAB36849 Fatp,Fatp1,FATP-1,Fatty acid transport protein 1,Long-chain fatty acid transport protein 1,Mouse,Mus musculus,Slc27a1,Solute carrier family 27 member 1
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
EIAAB36848 Bos taurus,Bovine,FATP1,FATP-1,Fatty acid transport protein 1,Long-chain fatty acid transport protein 1,SLC27A1,Solute carrier family 27 member 1
EIAAB36853 Acsvl3,Fatp3,FATP-3,Fatty acid transport protein 3,Long-chain fatty acid transport protein 3,Mouse,Mus musculus,Slc27a3,Solute carrier family 27 member 3
EIAAB36855 Acsvl4,Fatp4,FATP-4,Fatty acid transport protein 4,Long-chain fatty acid transport protein 4,Mouse,Mus musculus,Slc27a4,Solute carrier family 27 member 4
EIAAB36856 ACSVL4,FATP4,FATP-4,Fatty acid transport protein 4,Homo sapiens,Human,Long-chain fatty acid transport protein 4,SLC27A4,Solute carrier family 27 member 4
EIAAB36847 ACSVL5,FATP1,FATP-1,Fatty acid transport protein 1,Homo sapiens,Human,Long-chain fatty acid transport protein 1,SLC27A1,Solute carrier family 27 member 1
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
Y050476 Anti-ACSL3(long-chain fatty-acid-Coenzyme A ligase 3) Antibody 100ug
26-138 ACSL3 is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family c 0.05 mg
25-898 SLC27A2 is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family con 0.05 mg
27-706 ACSL1 encodes an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this fam 0.05 mg
27-705 ACSL1 encodes an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this fam 0.05 mg
GWB-E31BE4 Fatty-acid-coenzyme A Ligase Long-chain 3 (FACL3) (ACSL3) Rabbit anti-Human Polyclonal (N-Terminus) Antibody


 

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