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Leptin (Obesity factor)

 LEP_MOUSE               Reviewed;         167 AA.
P41160;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=Leptin;
AltName: Full=Obesity factor;
Flags: Precursor;
Name=Lep; Synonyms=Ob;
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=7984236; DOI=10.1038/372425a0;
Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
"Positional cloning of the mouse obese gene and its human homologue.";
Nature 372:425-432(1994).
[2]
ERRATUM.
Zhang Y., Proenca P., Maffei M., Barone M., Leopold L., Friedman J.M.;
Nature 374:479-479(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
Chehab F.F., Lim M.E.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8589726; DOI=10.1038/ng0396-318;
Chehab F.F., Lim M.E., Lu R.;
"Correction of the sterility defect in homozygous obese female mice by
treatment with the human recombinant leptin.";
Nat. Genet. 12:318-320(1996).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9732873; DOI=10.1038/29795;
Lord G.M., Matarese G., Howard J.K., Baker R.J., Bloom S.R.,
Lechler R.I.;
"Leptin modulates the T-cell immune response and reverses starvation-
induced immunosuppression.";
Nature 394:897-901(1998).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10660043; DOI=10.1016/S0092-8674(00)81558-5;
Ducy P., Amling M., Takeda S., Priemel M., Schilling A.F., Beil F.T.,
Shen J., Vinson C., Rueger J.M., Karsenty G.;
"Leptin inhibits bone formation through a hypothalamic relay: a
central control of bone mass.";
Cell 100:197-207(2000).
[7]
FUNCTION.
PubMed=11373681; DOI=10.1038/35078085;
Cowley M.A., Smart J.L., Rubinstein M., Cerdan M.G., Diano S.,
Horvath T.L., Cone R.D., Low M.J.;
"Leptin activates anorexigenic POMC neurons through a neural network
in the arcuate nucleus.";
Nature 411:480-484(2001).
[8]
FUNCTION.
PubMed=12594516; DOI=10.1038/nature01388;
Bates S.H., Stearns W.H., Dundon T.A., Schubert M., Tso A.W., Wang Y.,
Banks A.S., Lavery H.J., Haq A.K., Maratos-Flier E., Neel B.G.,
Schwartz M.W., Myers M.G. Jr.;
"STAT3 signalling is required for leptin regulation of energy balance
but not reproduction.";
Nature 421:856-859(2003).
[9]
REVIEW OF FUNCTION IN IMMUNITY.
PubMed=15122202; DOI=10.1038/nri1350;
La Cava A., Matarese G.;
"The weight of leptin in immunity.";
Nat. Rev. Immunol. 4:371-379(2004).
[10]
FUNCTION.
PubMed=15899045; DOI=10.1186/ar1708;
Otero M., Lago R., Lago F., Reino J.J., Gualillo O.;
"signaling pathway involved in nitric oxide synthase type II
activation in chondrocytes: synergistic effect of leptin with
interleukin-1.";
Arthritis Res. Ther. 7:R581-R591(2005).
[11]
FUNCTION.
PubMed=16825198; DOI=10.1074/jbc.M601991200;
Gonzalez R.R., Cherfils S., Escobar M., Yoo J.H., Carino C.,
Styer A.K., Sullivan B.T., Sakamoto H., Olawaiye A., Serikawa T.,
Lynch M.P., Rueda B.R.;
"Leptin signaling promotes the growth of mammary tumors and increases
the expression of vascular endothelial growth factor (VEGF) and its
receptor type two (VEGF-R2).";
J. Biol. Chem. 281:26320-26328(2006).
[12]
FUNCTION.
PubMed=20620997; DOI=10.1016/j.cmet.2010.05.010;
Ramadori G., Fujikawa T., Fukuda M., Anderson J., Morgan D.A.,
Mostoslavsky R., Stuart R.C., Perello M., Vianna C.R., Nillni E.A.,
Rahmouni K., Coppari R.;
"SIRT1 deacetylase in POMC neurons is required for homeostatic
defenses against diet-induced obesity.";
Cell Metab. 12:78-87(2010).
[13]
REVIEW OF FUNCTION.
PubMed=25232147; DOI=10.1530/JOE-14-0404;
Allison M.B., Myers M.G. Jr.;
"20 years of leptin: connecting leptin signaling to biological
function.";
J. Endocrinol. 223:T25-T35(2014).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25060689; DOI=10.1016/j.metabol.2014.06.010;
Cassano S., Pucino V., La Rocca C., Procaccini C., De Rosa V.,
Marone G., Matarese G.;
"Leptin modulates autophagy in human CD4+CD25- conventional T cells.";
Metabolism 63:1272-1279(2014).
[15]
FUNCTION.
PubMed=25383904; DOI=10.1038/nn.3861;
Flak J.N., Patterson C.M., Garfield A.S., D'Agostino G., Goforth P.B.,
Sutton A.K., Malec P.A., Wong J.M., Germani M., Jones J.C., Rajala M.,
Satin L., Rhodes C.J., Olson D.P., Kennedy R.T., Heisler L.K.,
Myers M.G. Jr.;
"Leptin-inhibited PBN neurons enhance responses to hypoglycemia in
negative energy balance.";
Nat. Neurosci. 17:1744-1750(2014).
-!- FUNCTION: Key player in the regulation of energy balance and body
weight control. Once released into the circulation, has central
and peripheral effects by binding LEPR, found in many tissues,
which results in the activation of several major signaling
pathways (PubMed:15899045, PubMed:16825198, PubMed:11373681,
PubMed:12594516, PubMed:20620997). In the hypothalamus, acts as an
appetite-regulating factor that induces a decrease in food intake
and an increase in energy consumption by inducing anorexinogenic
factors and suppressing orexigenic neuropeptides, also regulates
bone mass and secretion of hypothalamo-pituitary-adrenal hormones.
In the periphery, increases basal metabolism, influences
reproductive function, regulates pancreatic beta-cell function and
insulin secretion, is pro-angiogenic for endothelial cell and
affects innate and adaptive immunity (By similarity)
(PubMed:8589726, PubMed:10660043, PubMed:25383904,
PubMed:25060689, PubMed:9732873, PubMed:12594516). In the arcuate
nucleus of the hypothalamus, activates by depolarization POMC
neurons inducing FOS and SOCS3 expression to release anorexigenic
peptides and inhibits by hyperpolarization NPY neurons inducing
SOCS3 with a consequent reduction on release of orexigenic
peptides (By similarity) (PubMed:20620997, PubMed:11373681). In
addition to its known satiety inducing effect, has a modulatory
role in nutrient absorption. In the intestine, reduces glucose
absorption by enterocytes by activating PKC and leading to a
sequential activation of p38, PI3K and ERK signaling pathways
which exerts an inhibitory effect on glucose absorption. Acts as a
growth factor on certain tissues, through the activation of
different signaling pathways increases expression of genes
involved in cell cycle regulation such as CCND1, via JAK2-STAT3
pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By
similarity) (PubMed:16825198, PubMed:20620997). May also play an
apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5
expression (By similarity). Pro-angiogenic, has mitogenic activity
on vascular endothelial cells and plays a role in matrix
remodeling by regulating the expression of matrix
metalloproteinases (MMPs) and tissue inhibitors of
metalloproteinases (TIMPs) (PubMed:16825198). In innate immunity,
modulates the activity and function of neutrophils by increasing
chemotaxis and the secretion of oxygen radicals. Increases
phagocytosis by macrophages and enhances secretion of pro-
inflammatory mediators. Increases cytotoxic ability of NK cells
(Probable). Plays a pro-inflammatory role, in synergy with IL1B,
by inducing NOS2 wich promotes the production of IL6, IL8 and
Prostaglandin E2, through a signaling pathway that involves JAK2,
PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045). In adaptive
immunity, promotes the switch of memory T-cells towards T helper-1
cell immune responses (By similarity). Increases CD4(+)CD25(-) T
cells proliferation and reduces autophagy during TCR (T cell
receptor) stimulation, through MTOR signaling pathway activation
and BCL2 up-regulation (PubMed:25060689).
{ECO:0000250|UniProtKB:P41159, ECO:0000250|UniProtKB:P41160,
ECO:0000250|UniProtKB:P50596, ECO:0000269|PubMed:10660043,
ECO:0000269|PubMed:11373681, ECO:0000269|PubMed:12594516,
ECO:0000269|PubMed:15899045, ECO:0000269|PubMed:16825198,
ECO:0000269|PubMed:20620997, ECO:0000269|PubMed:25060689,
ECO:0000269|PubMed:25383904, ECO:0000269|PubMed:8589726,
ECO:0000269|PubMed:9732873, ECO:0000305|PubMed:15122202,
ECO:0000305|PubMed:25232147}.
-!- INTERACTION:
P48356:Lepr; NbExp=6; IntAct=EBI-16108810, EBI-2257257;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25232147}.
-!- DISEASE: Note=Defects in Lep are the cause of profound obesity and
type II diabetes.
-!- DISRUPTION PHENOTYPE: Mutants are severely obese and sterile
(PubMed:8589726). Animals have an increased bone formation leading
to high bone mass (PubMed:10660043). Have impaired T-cell
immunity, Th2 responses are favoured in mutants (PubMed:9732873).
CD4(+)CD25(-) T-cells of mutant mice show high levels of autophagy
(PubMed:25060689). {ECO:0000269|PubMed:10660043,
ECO:0000269|PubMed:25060689, ECO:0000269|PubMed:8589726,
ECO:0000269|PubMed:9732873}.
-!- SIMILARITY: Belongs to the leptin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U18812; AAA64564.1; -; mRNA.
EMBL; U22421; AAA64213.1; -; Genomic_DNA.
CCDS; CCDS19955.1; -.
PIR; S50863; LTMS.
RefSeq; NP_032519.1; NM_008493.3.
UniGene; Mm.277072; -.
ProteinModelPortal; P41160; -.
SMR; P41160; -.
BioGrid; 201138; 4.
CORUM; P41160; -.
DIP; DIP-60999N; -.
IntAct; P41160; 1.
STRING; 10090.ENSMUSP00000067046; -.
PhosphoSitePlus; P41160; -.
PaxDb; P41160; -.
PRIDE; P41160; -.
Ensembl; ENSMUST00000069789; ENSMUSP00000067046; ENSMUSG00000059201.
GeneID; 16846; -.
KEGG; mmu:16846; -.
UCSC; uc009bcv.1; mouse.
CTD; 3952; -.
MGI; MGI:104663; Lep.
eggNOG; ENOG410IVT0; Eukaryota.
eggNOG; ENOG410Y7NT; LUCA.
GeneTree; ENSGT00390000011772; -.
HOGENOM; HOG000252923; -.
HOVERGEN; HBG007860; -.
InParanoid; P41160; -.
KO; K05424; -.
OMA; QISNDLE; -.
OrthoDB; EOG091G0Y82; -.
PhylomeDB; P41160; -.
TreeFam; TF105086; -.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
PRO; PR:P41160; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000059201; -.
CleanEx; MM_LEP; -.
ExpressionAtlas; P41160; baseline and differential.
Genevisible; P41160; MM.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IDA:MGI.
GO; GO:0005179; F:hormone activity; IBA:GO_Central.
GO; GO:0051428; F:peptide hormone receptor binding; IBA:GO_Central.
GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IGI:MGI.
GO; GO:0008343; P:adult feeding behavior; IDA:HGNC.
GO; GO:0001525; P:angiogenesis; ISO:MGI.
GO; GO:0008206; P:bile acid metabolic process; IDA:MGI.
GO; GO:0098868; P:bone growth; IMP:UniProtKB.
GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:0071298; P:cellular response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IGI:MGI.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0042755; P:eating behavior; IGI:MGI.
GO; GO:0006112; P:energy reserve metabolic process; IBA:GO_Central.
GO; GO:0006635; P:fatty acid beta-oxidation; IGI:MGI.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IGI:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0006114; P:glycerol biosynthetic process; IEA:Ensembl.
GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IGI:MGI.
GO; GO:0032615; P:interleukin-12 production; IDA:UniProtKB.
GO; GO:0032635; P:interleukin-6 production; IDA:UniProtKB.
GO; GO:0072604; P:interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; ISS:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032099; P:negative regulation of appetite; IDA:HGNC.
GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
GO; GO:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
GO; GO:0070093; P:negative regulation of glucagon secretion; IDA:BHF-UCL.
GO; GO:0046325; P:negative regulation of glucose import; ISS:UniProtKB.
GO; GO:2000486; P:negative regulation of glutamine transport; IEA:Ensembl.
GO; GO:0010888; P:negative regulation of lipid storage; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045906; P:negative regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IDA:UniProtKB.
GO; GO:0001890; P:placenta development; ISO:MGI.
GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
GO; GO:1904651; P:positive regulation of fat cell apoptotic process; IEA:Ensembl.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IEA:Ensembl.
GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IDA:UniProtKB.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IDA:MGI.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISS:UniProtKB.
GO; GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:2000366; P:positive regulation of STAT protein import into nucleus; IDA:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:0032310; P:prostaglandin secretion; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0046850; P:regulation of bone remodeling; IMP:UniProtKB.
GO; GO:0090335; P:regulation of brown fat cell differentiation; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; IGI:MGI.
GO; GO:0006111; P:regulation of gluconeogenesis; IMP:MGI.
GO; GO:0050796; P:regulation of insulin secretion; IMP:MGI.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IDA:MGI.
GO; GO:0060587; P:regulation of lipoprotein lipid oxidation; IEA:Ensembl.
GO; GO:0019222; P:regulation of metabolic process; IMP:MGI.
GO; GO:0032814; P:regulation of natural killer cell activation; ISS:UniProtKB.
GO; GO:0042269; P:regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0032817; P:regulation of natural killer cell proliferation; ISS:UniProtKB.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0050810; P:regulation of steroid biosynthetic process; IMP:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0002021; P:response to dietary excess; IMP:MGI.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IMP:MGI.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0019953; P:sexual reproduction; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000065; Leptin.
PANTHER; PTHR11724; PTHR11724; 1.
Pfam; PF02024; Leptin; 1.
PIRSF; PIRSF001837; Leptin; 1.
PRINTS; PR00495; LEPTIN.
ProDom; PD005698; Leptin; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
Complete proteome; Diabetes mellitus; Disulfide bond; Obesity;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 167 Leptin.
/FTId=PRO_0000017687.
DISULFID 117 167 {ECO:0000250}.
VARIANT 49 49 Missing (in 30% the clones).
SEQUENCE 167 AA; 18709 MW; D6783E6C76FD7116 CRC64;
MCWRPLCRFL WLWSYLSYVQ AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL
DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP
QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC


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