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Fatty acid-binding protein, adipocyte (3T3-L1 lipid-binding protein) (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (A-FABP) (AFABP) (Fatty acid-binding protein 4) (Myelin P2 protein homolog) (P15) (P2 adipocyte protein) (Protein 422)

 FABP4_MOUSE             Reviewed;         132 AA.
P04117;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 187.
RecName: Full=Fatty acid-binding protein, adipocyte;
AltName: Full=3T3-L1 lipid-binding protein;
AltName: Full=Adipocyte lipid-binding protein;
Short=ALBP;
AltName: Full=Adipocyte-type fatty acid-binding protein;
Short=A-FABP;
Short=AFABP;
AltName: Full=Fatty acid-binding protein 4;
AltName: Full=Myelin P2 protein homolog;
AltName: Full=P15;
AltName: Full=P2 adipocyte protein;
AltName: Full=Protein 422;
Name=Fabp4; Synonyms=Ap2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6206497; DOI=10.1073/pnas.81.17.5468;
Bernlohr D.A., Angus C.W., Lane M.D., Bolanowski M.A., Kelly T.J. Jr.;
"Expression of specific mRNAs during adipose differentiation:
identification of an mRNA encoding a homologue of myelin P2 protein.";
Proc. Natl. Acad. Sci. U.S.A. 81:5468-5472(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3520554; DOI=10.1073/pnas.83.11.3786;
Hunt C.R., Ro J.H.-S., Dobson D.E., Min H.Y., Spiegelman B.M.;
"Adipocyte P2 gene: developmental expression and homology of 5'-
flanking sequences among fat cell-specific genes.";
Proc. Natl. Acad. Sci. U.S.A. 83:3786-3790(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3015943;
Phillips M., Djian P., Green H.;
"The nucleotide sequence of three genes participating in the adipose
differentiation of 3T3 cells.";
J. Biol. Chem. 261:10821-10827(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
[6]
PROTEIN SEQUENCE OF 2-132.
PubMed=2844775;
Matarese V., Bernlohr D.A.;
"Purification of murine adipocyte lipid-binding protein.
Characterization as a fatty acid- and retinoic acid-binding protein.";
J. Biol. Chem. 263:14544-14551(1988).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2452440; DOI=10.1073/pnas.85.9.2949;
Cook J.S., Lucas J.J., Sibley E., Bolanowski M.A., Christy R.J.,
Kelly T.J. Jr., Lane M.D.;
"Expression of the differentiation-induced gene for fatty acid-binding
protein is activated by glucocorticoid and cAMP.";
Proc. Natl. Acad. Sci. U.S.A. 85:2949-2953(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-132.
PubMed=3968175; DOI=10.1083/jcb.100.2.514;
Cook K.S., Hunt C.R., Spiegelman B.M.;
"Developmentally regulated mRNAs in 3T3-adipocytes: analysis of
transcriptional control.";
J. Cell Biol. 100:514-520(1985).
[9]
PROTEIN SEQUENCE OF 25-35; 37-51 AND 59-88.
TISSUE=Mammary gland;
PubMed=8447836; DOI=10.1006/bbrc.1993.1184;
Bansal M.P., Medina D.;
"Expression of fatty acid-binding proteins in the developing mouse
mammary gland.";
Biochem. Biophys. Res. Commun. 191:61-69(1993).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPARG.
PubMed=12077340; DOI=10.1128/MCB.22.14.5114-5127.2002;
Tan N.-S., Shaw N.S., Vinckenbosch N., Liu P., Yasmin R.,
Desvergne B., Wahli W., Noy N.;
"Selective cooperation between fatty acid binding proteins and
peroxisome proliferator-activated receptors in regulating
transcription.";
Mol. Cell. Biol. 22:5114-5127(2002).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPARG.
PubMed=16574478; DOI=10.1016/j.bbalip.2006.02.006;
Adida A., Spener F.;
"Adipocyte-type fatty acid-binding protein as inter-compartmental
shuttle for peroxisome proliferator activated receptor gamma agonists
in cultured cell.";
Biochim. Biophys. Acta 1761:172-181(2006).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-22; ARG-31;
LYS-32; LEU-67; LEU-87 AND LEU-92.
PubMed=17516629; DOI=10.1021/bi700047a;
Ayers S.D., Nedrow K.L., Gillilan R.E., Noy N.;
"Continuous nucleocytoplasmic shuttling underlies transcriptional
activation of PPARgamma by FABP4.";
Biochemistry 46:6744-6752(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1554730; DOI=10.1021/bi00128a024;
Xu Z., Bernlohr D.A., Banaszak L.J.;
"Crystal structure of recombinant murine adipocyte lipid-binding
protein.";
Biochemistry 31:3484-3492(1992).
[15]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=8463311;
Xu Z., Bernlohr D.A., Banaszak L.J.;
"The adipocyte lipid-binding protein at 1.6-A resolution. Crystal
structures of the apoprotein and with bound saturated and unsaturated
fatty acids.";
J. Biol. Chem. 268:7874-7884(1993).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=10423455; DOI=10.1016/S0006-3495(99)76961-4;
Ory J.J., Banaszak L.J.;
"Studies of the ligand binding reaction of adipocyte lipid binding
protein using the fluorescent probe 1, 8-anilinonaphthalene-8-
sulfonate.";
Biophys. J. 77:1107-1116(1999).
[17]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
PubMed=8161548; DOI=10.1021/bi00182a017;
LaLonde J.M., Bernlohr D.A., Banaszak L.J.;
"X-ray crystallographic structures of adipocyte lipid-binding protein
complexed with palmitate and hexadecanesulfonic acid. Properties of
cavity binding sites.";
Biochemistry 33:4885-4895(1994).
[18]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
PubMed=7929228;
LaLonde J.M., Levenson M.A., Roe J.J., Bernlohr D.A., Banaszak L.J.;
"Adipocyte lipid-binding protein complexed with arachidonic acid.
Titration calorimetry and X-ray crystallographic studies.";
J. Biol. Chem. 269:25339-25347(1994).
[19]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH FATTY ACID.
PubMed=14594993; DOI=10.1194/jlr.M300113-JLR200;
Reese A.J., Banaszak L.J.;
"Specificity determinants for lipids bound to beta-barrel proteins.";
J. Lipid Res. 45:232-243(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH TROGLITAZONE
AND LINOLEIC ACID, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PHE-58; LEU-67; LEU-87 AND LEU-92.
PubMed=17761196; DOI=10.1016/j.jmb.2007.07.040;
Gillilan R.E., Ayers S.D., Noy N.;
"Structural basis for activation of fatty acid-binding protein 4.";
J. Mol. Biol. 372:1246-1260(2007).
-!- FUNCTION: Lipid transport protein in adipocytes. Binds both long
chain fatty acids and retinoic acid. Delivers long-chain fatty
acids and retinoic acid to their cognate receptors in the nucleus.
{ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478,
ECO:0000269|PubMed:17516629}.
-!- SUBUNIT: Monomer (By similarity). Homodimer. Interacts with PPARG.
{ECO:0000250, ECO:0000269|PubMed:12077340,
ECO:0000269|PubMed:14594993, ECO:0000269|PubMed:16574478,
ECO:0000269|PubMed:17761196, ECO:0000269|PubMed:7929228,
ECO:0000269|PubMed:8161548}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17516629,
ECO:0000269|PubMed:17761196}. Nucleus
{ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}.
Note=Depending on the nature of the ligand, a conformation change
exposes a nuclear localization motif and the protein is
transported into the nucleus (PubMed:17516629). Subject to
constitutive nuclear export (PubMed:17516629, PubMed:17761196).
{ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates the
hydrophobic ligand in its interior.
-!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
protein (FABP) family. {ECO:0000305}.
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EMBL; K02109; AAA39416.1; -; mRNA.
EMBL; M13264; AAA39870.1; -; Genomic_DNA.
EMBL; M13261; AAA39870.1; JOINED; Genomic_DNA.
EMBL; M13262; AAA39870.1; JOINED; Genomic_DNA.
EMBL; M13263; AAA39870.1; JOINED; Genomic_DNA.
EMBL; M13385; AAA39417.1; -; Genomic_DNA.
EMBL; AK003143; BAB22601.1; -; mRNA.
EMBL; BC054426; AAH54426.1; -; mRNA.
EMBL; M20497; AAA37188.1; -; Genomic_DNA.
EMBL; M28726; AAA37112.1; -; mRNA.
CCDS; CCDS17238.1; -.
PIR; B25952; B25952.
RefSeq; NP_077717.1; NM_024406.2.
UniGene; Mm.582; -.
PDB; 1A18; X-ray; 2.40 A; A=2-132.
PDB; 1A2D; X-ray; 2.40 A; A/B=2-132.
PDB; 1AB0; X-ray; 1.90 A; A=3-132.
PDB; 1ACD; X-ray; 2.70 A; A=3-132.
PDB; 1ADL; X-ray; 1.60 A; A=2-132.
PDB; 1ALB; X-ray; 2.50 A; A=2-132.
PDB; 1G74; X-ray; 1.70 A; A=2-132.
PDB; 1G7N; X-ray; 1.50 A; A=2-132.
PDB; 1LIB; X-ray; 1.70 A; A=2-132.
PDB; 1LIC; X-ray; 1.60 A; A=2-132.
PDB; 1LID; X-ray; 1.60 A; A=2-132.
PDB; 1LIE; X-ray; 1.60 A; A=2-132.
PDB; 1LIF; X-ray; 1.60 A; A=2-132.
PDB; 2ANS; X-ray; 2.50 A; A/B=2-132.
PDB; 2Q9S; X-ray; 2.30 A; A=1-132.
PDB; 2QM9; X-ray; 2.31 A; A/B=1-132.
PDB; 3HK1; X-ray; 1.70 A; A=2-132.
PDB; 3JS1; X-ray; 1.81 A; A/B=2-132.
PDB; 3JSQ; X-ray; 2.30 A; A=2-132.
PDB; 5C0N; X-ray; 3.00 A; A/B=1-132.
PDB; 5D8J; X-ray; 3.00 A; A=1-132.
PDBsum; 1A18; -.
PDBsum; 1A2D; -.
PDBsum; 1AB0; -.
PDBsum; 1ACD; -.
PDBsum; 1ADL; -.
PDBsum; 1ALB; -.
PDBsum; 1G74; -.
PDBsum; 1G7N; -.
PDBsum; 1LIB; -.
PDBsum; 1LIC; -.
PDBsum; 1LID; -.
PDBsum; 1LIE; -.
PDBsum; 1LIF; -.
PDBsum; 2ANS; -.
PDBsum; 2Q9S; -.
PDBsum; 2QM9; -.
PDBsum; 3HK1; -.
PDBsum; 3JS1; -.
PDBsum; 3JSQ; -.
PDBsum; 5C0N; -.
PDBsum; 5D8J; -.
ProteinModelPortal; P04117; -.
SMR; P04117; -.
IntAct; P04117; 1.
MINT; P04117; -.
STRING; 10090.ENSMUSP00000029041; -.
ChEMBL; CHEMBL1075118; -.
GuidetoPHARMACOLOGY; 2534; -.
CarbonylDB; P04117; -.
iPTMnet; P04117; -.
PhosphoSitePlus; P04117; -.
SWISS-2DPAGE; P04117; -.
PaxDb; P04117; -.
PeptideAtlas; P04117; -.
PRIDE; P04117; -.
Ensembl; ENSMUST00000029041; ENSMUSP00000029041; ENSMUSG00000062515.
GeneID; 11770; -.
KEGG; mmu:11770; -.
UCSC; uc008opl.2; mouse.
CTD; 2167; -.
MGI; MGI:88038; Fabp4.
eggNOG; KOG4015; Eukaryota.
eggNOG; ENOG4111US8; LUCA.
GeneTree; ENSGT00760000118898; -.
HOGENOM; HOG000004829; -.
HOVERGEN; HBG005633; -.
InParanoid; P04117; -.
KO; K08753; -.
OMA; ATRKMAG; -.
OrthoDB; EOG091G0QSV; -.
PhylomeDB; P04117; -.
TreeFam; TF316894; -.
Reactome; R-MMU-163560; Triglyceride catabolism.
ChiTaRS; Tfap2a; mouse.
EvolutionaryTrace; P04117; -.
PRO; PR:P04117; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000062515; Expressed in 220 organ(s), highest expression level in lymph node.
CleanEx; MM_FABP4; -.
ExpressionAtlas; P04117; baseline and differential.
Genevisible; P04117; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051427; F:hormone receptor binding; IPI:UniProtKB.
GO; GO:0036041; F:long-chain fatty acid binding; IDA:UniProtKB.
GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
GO; GO:0001816; P:cytokine production; IMP:MGI.
GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
GO; GO:0015909; P:long-chain fatty acid transport; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
GO; GO:0050872; P:white fat cell differentiation; IDA:MGI.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR033073; FABP4.
InterPro; IPR000463; Fatty_acid-bd.
InterPro; IPR031259; ILBP.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11955; PTHR11955; 1.
PANTHER; PTHR11955:SF83; PTHR11955:SF83; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00178; FATTYACIDBP.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00214; FABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Lipid-binding; Nucleus; Phosphoprotein;
Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2844775}.
CHAIN 2 132 Fatty acid-binding protein, adipocyte.
{ECO:0000269|PubMed:2844775}.
/FTId=PRO_0000067367.
REGION 127 129 Fatty acid binding.
MOTIF 22 32 Nuclear localization signal.
{ECO:0000269|PubMed:17516629}.
MOD_RES 2 2 N-acetylcysteine.
{ECO:0000250|UniProtKB:P15090}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 20 20 Phosphotyrosine; by Tyr-kinases.
{ECO:0000250}.
MUTAGEN 22 22 K->A: Abolishes ligand-induced
translocation to the nucleus; when
associated with A-31 and A-32.
{ECO:0000269|PubMed:17516629}.
MUTAGEN 31 31 R->A: Abolishes ligand-induced
translocation to the nucleus; when
associated with A-22 and A-32.
{ECO:0000269|PubMed:17516629}.
MUTAGEN 32 32 K->A: Abolishes ligand-induced
translocation to the nucleus; when
associated with A-22 and A-31.
{ECO:0000269|PubMed:17516629}.
MUTAGEN 58 58 F->A: Abolishes ligand-induced
translocation to the nucleus.
{ECO:0000269|PubMed:17761196}.
MUTAGEN 67 67 L->A: Abolishes export from nucleus; when
associated with A-87 and A-92.
{ECO:0000269|PubMed:17516629,
ECO:0000269|PubMed:17761196}.
MUTAGEN 87 87 L->A: Abolishes export from nucleus; when
associated with A-67 and A-92.
{ECO:0000269|PubMed:17516629,
ECO:0000269|PubMed:17761196}.
MUTAGEN 92 92 L->A: Abolishes export from nucleus; when
associated with A-67 and A-87.
{ECO:0000269|PubMed:17516629,
ECO:0000269|PubMed:17761196}.
CONFLICT 40 40 N -> T (in Ref. 1; AAA39870).
{ECO:0000305}.
CONFLICT 111 111 G -> V (in Ref. 2; AAA39417).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:1G7N}.
STRAND 7 16 {ECO:0000244|PDB:1G7N}.
HELIX 17 24 {ECO:0000244|PDB:1G7N}.
HELIX 28 37 {ECO:0000244|PDB:1G7N}.
STRAND 41 46 {ECO:0000244|PDB:1G7N}.
STRAND 49 54 {ECO:0000244|PDB:1G7N}.
STRAND 61 65 {ECO:0000244|PDB:1G7N}.
STRAND 67 69 {ECO:0000244|PDB:5D8J}.
STRAND 71 74 {ECO:0000244|PDB:1G7N}.
STRAND 80 88 {ECO:0000244|PDB:1G7N}.
STRAND 91 98 {ECO:0000244|PDB:1G7N}.
STRAND 101 110 {ECO:0000244|PDB:1G7N}.
STRAND 113 120 {ECO:0000244|PDB:1G7N}.
STRAND 123 131 {ECO:0000244|PDB:1G7N}.
SEQUENCE 132 AA; 14650 MW; ED08EDDBBE2D7E32 CRC64;
MCDAFVGTWK LVSSENFDDY MKEVGVGFAT RKVAGMAKPN MIISVNGDLV TIRSESTFKN
TEISFKLGVE FDEITADDRK VKSIITLDGG ALVQVQKWDG KSTTIKRKRD GDKLVVECVM
KGVTSTRVYE RA


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E0184h ELISA kit Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Homo sapiens,Human 96T
E0184h ELISA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Homo sapiens,Human 96T
E0184r ELISA kit Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Rat,Rattus norvegicus 96T
E0184r ELISA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Rat,Rattus norvegicus 96T
E0184b ELISA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Bos taurus,Bovine,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte 96T
E0184b ELISA kit Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Bos taurus,Bovine,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte 96T
U0184r CLIA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Rat,Rattus norvegicus 96T
U0184b CLIA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Bos taurus,Bovine,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte 96T
U0184p CLIA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,AP2,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Pig,Sus scrofa 96T
E0184p ELISA Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,AP2,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Pig,Sus scrofa 96T
E0184p ELISA kit Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,AP2,FABP4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocyte,Pig,Sus scrofa 96T
U0184m CLIA 3T3-L1 lipid-binding protein,Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Ap2,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipocy 96T
E0184m ELISA 3T3-L1 lipid-binding protein,Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Ap2,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, adipoc 96T
E0184m ELISA kit 3T3-L1 lipid-binding protein,Adipocyte lipid-binding protein,Adipocyte-type fatty acid-binding protein,AFABP,A-FABP,ALBP,Ap2,Fabp4,Fatty acid-binding protein 4,Fatty acid-binding protein, a 96T
10-663-45676 Adipocyte Fatty Acid Binding Protein 4 (FABP4) Human - AFABP; Adipocyte lipid-binding protein; ALBP; A-FABP N_A 1 mg
10-663-45676 Adipocyte Fatty Acid Binding Protein 4 (FABP4) Human - AFABP; Adipocyte lipid-binding protein; ALBP; A-FABP N_A 0.01 mg
10-663-45676 Adipocyte Fatty Acid Binding Protein 4 (FABP4) Human - AFABP; Adipocyte lipid-binding protein; ALBP; A-FABP N_A 0.002 mg
18-272-196020 Fatty Acid Binding Protein 4 - Rabbit polyclonal to Fatty Acid Binding Protein 4; AFABP; Adipocyte lipid-binding protein; ALBP; A-FABP Polyclonal 0.05 mg
orb82641 Fatty-acid binding protein 4 His tag protein Fatty-acid binding protein 4(FABP4), also termed adipocyte fatty-acid binding protein (A-FABP), or aP2, is a novel adipocyte-expressed factor which account 100
orb82640 Fatty-acid binding protein 4 His tag protein Fatty-acid binding protein 4(FABP4), also termed adipocyte fatty-acid binding protein (A-FABP), or aP2, is a novel adipocyte-expressed factor which account 100
E0344b ELISA kit Bos taurus,Bovine,Differentiation-associated lipid-binding protein LP2,E-FABP,Epidermal-type fatty acid-binding protein,FABP5,Fatty acid-binding protein 5,Fatty acid-binding protein, epider 96T
U0344m CLIA E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus musculus,PA- 96T
E0344m ELISA E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus musculus,PA 96T
E0344m ELISA kit E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus muscul 96T


 

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