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Leptin receptor (LEP-R) (OB receptor) (OB-R) (CD antigen CD295)

 LEPR_RAT                Reviewed;        1162 AA.
Q62959; O35772; O35773; O54805; P70493; P70494; P70495; P97589;
Q62960; Q63007; Q63385; Q63386; Q9ERI4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Leptin receptor;
Short=LEP-R;
AltName: Full=OB receptor;
Short=OB-R;
AltName: CD_antigen=CD295;
Flags: Precursor;
Name=Lepr; Synonyms=Fa, Obr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT FA PRO-269.
STRAIN=Zucker; TISSUE=Hypothalamus;
PubMed=8673096; DOI=10.1038/ng0596-18;
Phillips M.S., Liu Q., Hammond H.A., Dugan V., Hey P.J., Caskey C.T.,
Hess J.F.;
"Leptin receptor missense mutation in the fatty Zucker rat.";
Nat. Genet. 13:18-19(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT FA PRO-269.
STRAIN=Sprague-Dawley, and Zucker fatty; TISSUE=Brain;
PubMed=8702432; DOI=10.1006/bbrc.1996.1070;
Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.;
"Substitution at codon 269 (glutamine --> proline) of the leptin
receptor (OB-R) cDNA is the only mutation found in the Zucker fatty
(fa/fa) rat.";
Biochem. Biophys. Res. Commun. 224:597-604(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND E), AND VARIANT FA
PRO-269.
STRAIN=Sprague-Dawley, and Zucker fatty;
PubMed=8769097; DOI=10.1006/bbrc.1996.1133;
Takaya K., Ogawa Y., Isse N., Okazaki T., Satoh N., Masuzaki H.,
Mori K., Tamura N., Hosoda K., Nakao K.;
"Molecular cloning of rat leptin receptor isoform complementary DNAs
-- identification of a missense mutation in Zucker fatty (fa/fa)
rats.";
Biochem. Biophys. Res. Commun. 225:75-83(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Karlsson C., Lindell K., Robinson I.C.A.F., Carlsson L.M.S.,
Carlsson B.;
"Cloning of the rat leptin receptor.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT FA PRO-269.
STRAIN=Sprague-Dawley, and Zucker fatty;
PubMed=8630068; DOI=10.1006/bbrc.1996.0691;
Iida M., Murakami T., Ishida K., Mizuno A., Kuwajima M., Shima K.;
"Phenotype-linked amino acid alteration in leptin receptor cDNA from
Zucker fatty (fa/fa) rat.";
Biochem. Biophys. Res. Commun. 222:19-26(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
STRAIN=Sprague-Dawley; TISSUE=Spleen;
Park J.H., Ju S.K., Na S.Y., You K.H., Kim K.L.;
"Molecular cloning, sequencing, and recombinant expression of the long
form of the rat leptin receptor isolated from whole spleen RNA.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=8772180; DOI=10.1016/0014-5793(96)00790-9;
Wang M.-Y., Zhou Y.T., Newgard C.B., Unger R.H.;
"A novel leptin receptor isoform in rat.";
FEBS Lett. 392:87-90(1996).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123.
Morishita T., Hidaka T., Kuzuyama T., Noguchi T.;
"Analysis of rat leptin receptor gene.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 557-802 AND 843-892 (ISOFORMS C AND E).
STRAIN=Sprague-Dawley;
PubMed=9268737; DOI=10.1006/bbrc.1997.7159;
Chien E.K., Hara M., Rouard M., Yano H., Phillippe M., Polonsky K.S.,
Bell G.I.;
"Increase in serum leptin and uterine leptin receptor messenger RNA
levels during pregnancy in rats.";
Biochem. Biophys. Res. Commun. 237:476-480(1997).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 694-878.
STRAIN=Sprague-Dawley; TISSUE=Pancreas;
Ma Z.;
"Identification of a leptin receptor in islet.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 821-894 (ISOFORM A).
STRAIN=Wistar Munich; TISSUE=Kidney;
Totsune K., Takahashi K., Mackenzie H.S., Murakami O., Arihara Z.,
Sone M., Satoh F., Mouri T., Brenner B.M., Ito S.;
"Leptin receptor gene expression in rat kidney.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[12]
FUNCTION (ISOFORM A).
PubMed=10698121; DOI=10.1016/S0196-9781(99)00156-4;
Kastin A.J., Pan W., Maness L.M., Koletsky R.J., Ernsberger P.;
"Decreased transport of leptin across the blood-brain barrier in rats
lacking the short form of the leptin receptor.";
Peptides 20:1449-1453(1999).
[13]
TISSUE SPECIFICITY.
PubMed=11861497; DOI=10.1210/endo.143.3.8669;
Hileman S.M., Pierroz D.D., Masuzaki H., Bjoerbaek C., El-Haschimi K.,
Banks W.A., Flier J.S.;
"Characterizaton of short isoforms of the leptin receptor in rat
cerebral microvessels and of brain uptake of leptin in mouse models of
obesity.";
Endocrinology 143:775-783(2002).
[14]
REVIEW ON FUNCTION, AND SUBUNIT.
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).
[15]
VARIANT FA PRO-269.
PubMed=8690163; DOI=10.2337/diab.45.8.1141;
Chua S.C. Jr., White D.W., Wu-Peng X.S., Liu S.M., Okada N.,
Kershaw E.E., Chung W.K., Power-Kehoe L., Chua M., Tartaglia L.A.,
Leibel R.L.;
"Phenotype of fatty due to Gln269Pro mutation in the leptin receptor
(Lepr).";
Diabetes 45:1141-1143(1996).
-!- FUNCTION: Receptor for hormone LEP/leptin (Probable). On ligand
binding, mediates LEP central and peripheral effects through the
activation of different signaling pathways such as JAK2/STAT3 and
MAPK cascade/FOS. In the hypothalamus, LEP 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
(PubMed:8690163). In the periphery, increases basal metabolism,
influences reproductive function, regulates pancreatic beta-cell
function and insulin secretion, is pro-angiogenic and affects
innate and adaptive immunity (By similarity). Control of energy
homeostasis and melanocortin production (stimulation of POMC and
full repression of AgRP transcription) is mediated by STAT3
signaling, whereas distinct signals regulate NPY and the control
of fertility, growth and glucose homeostasis. Involved in the
regulation of counter-regulatory response to hypoglycemia by
inhibiting neurons of the parabrachial nucleus. Has a specific
effect on T lymphocyte responses, differentially regulating the
proliferation of naive and memory T-cells. Leptin increases Th1
and suppresses Th2 cytokine production (By similarity).
{ECO:0000250|UniProtKB:P48356, ECO:0000250|UniProtKB:P48357,
ECO:0000269|PubMed:8690163, ECO:0000305|PubMed:25232147}.
-!- FUNCTION: Isoform A: May transport LEP across the blood-brain
barrier. Binds LEP and mediates LEP endocytosis (PubMed:10698121).
Does not induce phosphorylation of and activate STAT3 (By
similarity). {ECO:0000250|UniProtKB:P48356,
ECO:0000269|PubMed:10698121}.
-!- FUNCTION: Isoform E: Antagonizes Isoform A and isoform B-mediated
LEP binding and endocytosis. {ECO:0000250|UniProtKB:P48356}.
-!- SUBUNIT: Present as a mixture of monomers and dimers (Probable).
The phosphorylated receptor binds a number of SH2 domain-
containing proteins such as JAK2, STAT3, PTPN11, and SOCS3 (By
similarity). Interaction with SOCS3 inhibits JAK/STAT signaling
and MAPK cascade (By similarity). {ECO:0000250|UniProtKB:P48356,
ECO:0000250|UniProtKB:P48357, ECO:0000305|PubMed:25232147}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P48357}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P48357}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P48357}.
-!- SUBCELLULAR LOCATION: Isoform E: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=B;
IsoId=Q62959-1; Sequence=Displayed;
Name=A;
IsoId=Q62959-2; Sequence=VSP_001705, VSP_001706;
Name=C;
IsoId=Q62959-3; Sequence=VSP_001707, VSP_001708;
Name=D;
IsoId=Q62959-6; Sequence=Not described;
Name=E;
IsoId=Q62959-4; Sequence=VSP_001709, VSP_001710;
Name=F;
IsoId=Q62959-5; Sequence=VSP_001711, VSP_001712;
-!- TISSUE SPECIFICITY: Isoform B is expressed in kidney, liver, lung,
ovary, spleen and uterus. Increased level in uterus during
gestation (PubMed:8772180). Isoform A and isoform C are
predominantly expressed in cerebral microvessels and choroid
plexus, with lower levels in cortex, cerebellum and hypothalamus
but also liver and lung (PubMed:11861497). Isoform F is expressed
at high levels in brain, liver and spleen and less in stomach,
kidney, thymus, heart, lung and hypothalamus (PubMed:11861497,
PubMed:8772180). {ECO:0000269|PubMed:11861497,
ECO:0000269|PubMed:8772180}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: On ligand binding, phosphorylated on two conserved C-terminal
tyrosine residues (isoform B only) by JAK2. Tyr-985 is required
for complete binding and activation of PTPN11, ERK/FOS
activation,for interaction with SOCS3 and SOCS3 mediated
inhibition of leptin signaling. Phosphorylation on Tyr-1138 is
required for STAT3 binding/activation. Phosphorylation of Tyr-1077
has a more accessory role. {ECO:0000250|UniProtKB:P48356}.
-!- DISEASE: Note=The fatty (Fa) mutation produces profound obesity of
early onset caused by hyperphagia, defective non-shivering
thermogenesis, and preferential deposition of energy into adipose
tissue.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
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EMBL; U52966; AAC52587.1; -; mRNA.
EMBL; D84550; BAA12697.1; -; mRNA.
EMBL; D84551; BAA12698.1; -; mRNA.
EMBL; D85557; BAA12830.1; -; mRNA.
EMBL; D85558; BAA12831.1; -; mRNA.
EMBL; D85559; BAA12832.1; -; mRNA.
EMBL; U60151; AAB06616.1; -; mRNA.
EMBL; D84125; BAA12230.1; -; mRNA.
EMBL; D84126; BAA12231.1; -; mRNA.
EMBL; AF287268; AAF89300.1; -; mRNA.
EMBL; U53144; AAB03088.1; -; mRNA.
EMBL; AB011006; BAA24899.1; -; Genomic_DNA.
EMBL; AF007818; AAB63201.1; -; mRNA.
EMBL; AF007819; AAB63202.1; -; mRNA.
EMBL; U67207; AAB40654.1; -; mRNA.
EMBL; AF304191; AAG22823.1; -; mRNA.
PIR; JC4895; PC4184.
PIR; S74225; S74225.
RefSeq; NP_036728.1; NM_012596.1. [Q62959-1]
UniGene; Rn.9891; -.
ProteinModelPortal; Q62959; -.
SMR; Q62959; -.
BioGrid; 246689; 1.
STRING; 10116.ENSRNOP00000046647; -.
iPTMnet; Q62959; -.
PhosphoSitePlus; Q62959; -.
PaxDb; Q62959; -.
PRIDE; Q62959; -.
GeneID; 24536; -.
KEGG; rno:24536; -.
CTD; 3953; -.
RGD; 3001; Lepr.
eggNOG; ENOG410IKH4; Eukaryota.
eggNOG; ENOG4110JZP; LUCA.
HOVERGEN; HBG000140; -.
InParanoid; Q62959; -.
KO; K05062; -.
PhylomeDB; Q62959; -.
PRO; PR:Q62959; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0038021; F:leptin receptor activity; ISS:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
GO; GO:0016500; F:protein-hormone receptor activity; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IMP:RGD.
GO; GO:0098868; P:bone growth; ISS:UniProtKB.
GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
GO; GO:0042755; P:eating behavior; IMP:RGD.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:RGD.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:1903999; P:negative regulation of eating behavior; IMP:RGD.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:RGD.
GO; GO:0051346; P:negative regulation of hydrolase activity; ISO:RGD.
GO; GO:1904060; P:negative regulation of locomotor rhythm; IMP:RGD.
GO; GO:0001542; P:ovulation from ovarian follicle; IEP:RGD.
GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0044321; P:response to leptin; IEP:RGD.
GO; GO:0033993; P:response to lipid; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; IEP:RGD.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
InterPro; IPR015752; Lep_receptor.
PANTHER; PTHR23036:SF109; PTHR23036:SF109; 3.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 3.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Membrane; Obesity;
Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1162 Leptin receptor.
/FTId=PRO_0000010908.
TOPO_DOM 22 839 Extracellular. {ECO:0000255}.
TRANSMEM 840 860 Helical. {ECO:0000255}.
TOPO_DOM 861 1162 Cytoplasmic. {ECO:0000255}.
DOMAIN 238 331 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 537 632 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 637 729 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 738 831 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 465 482 Leptin-binding.
{ECO:0000250|UniProtKB:P48357}.
REGION 891 896 Required for JAK2 activation.
{ECO:0000250|UniProtKB:P48356}.
REGION 896 904 Required for STAT3 phosphorylation.
{ECO:0000250|UniProtKB:P48356}.
MOTIF 620 624 WSXWS motif.
MOTIF 869 877 Box 1 motif.
MOD_RES 880 880 Phosphoserine.
{ECO:0000250|UniProtKB:P48357}.
MOD_RES 985 985 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1077 1077 Phosphotyrosine.
{ECO:0000250|UniProtKB:P48356}.
MOD_RES 1138 1138 Phosphotyrosine; by JAK2.
{ECO:0000250|UniProtKB:P48356}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 686 686 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 698 698 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 726 726 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 90 {ECO:0000250|UniProtKB:P48357}.
DISULFID 89 99 {ECO:0000250|UniProtKB:P48357}.
DISULFID 131 142 {ECO:0000250|UniProtKB:P48357}.
DISULFID 186 195 {ECO:0000250|UniProtKB:P48357}.
DISULFID 188 193 {ECO:0000250|UniProtKB:P48357}.
DISULFID 350 410 {ECO:0000250|UniProtKB:P48357}.
DISULFID 411 416 {ECO:0000250|UniProtKB:P48357}.
DISULFID 434 445 {ECO:0000250|UniProtKB:P48357}.
DISULFID 471 526 {ECO:0000250|UniProtKB:P48357}.
DISULFID 486 496 {ECO:0000250|UniProtKB:P48357}.
VAR_SEQ 797 805 DNFIPIEKY -> GMCTVLLLN (in isoform E).
{ECO:0000303|PubMed:8769097,
ECO:0000303|PubMed:9268737}.
/FTId=VSP_001709.
VAR_SEQ 806 1162 Missing (in isoform E).
{ECO:0000303|PubMed:8769097,
ECO:0000303|PubMed:9268737}.
/FTId=VSP_001710.
VAR_SEQ 890 895 PETFEH -> IMPGRN (in isoform F).
{ECO:0000303|PubMed:8772180}.
/FTId=VSP_001711.
VAR_SEQ 890 894 PETFE -> RADTL (in isoform A).
{ECO:0000303|PubMed:8630068,
ECO:0000303|PubMed:8769097,
ECO:0000303|Ref.11}.
/FTId=VSP_001705.
VAR_SEQ 890 892 PET -> VTV (in isoform C).
{ECO:0000303|PubMed:9268737}.
/FTId=VSP_001707.
VAR_SEQ 893 1162 Missing (in isoform C).
{ECO:0000303|PubMed:9268737}.
/FTId=VSP_001708.
VAR_SEQ 895 1162 Missing (in isoform A).
{ECO:0000303|PubMed:8630068,
ECO:0000303|PubMed:8769097,
ECO:0000303|Ref.11}.
/FTId=VSP_001706.
VAR_SEQ 896 1162 Missing (in isoform F).
{ECO:0000303|PubMed:8772180}.
/FTId=VSP_001712.
VARIANT 269 269 Q -> P (in FA).
{ECO:0000269|PubMed:8630068,
ECO:0000269|PubMed:8673096,
ECO:0000269|PubMed:8690163,
ECO:0000269|PubMed:8702432,
ECO:0000269|PubMed:8769097}.
CONFLICT 2 2 T -> M (in Ref. 4; AAB06616).
{ECO:0000305}.
CONFLICT 12 12 H -> P (in Ref. 8; BAA24899).
{ECO:0000305}.
CONFLICT 34 34 K -> R (in Ref. 8; BAA24899).
{ECO:0000305}.
CONFLICT 415 417 ACH -> QCQ (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 422 422 E -> D (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 493 493 F -> L (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 498 498 F -> S (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 612 612 R -> Q (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 690 690 S -> T (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 703 704 WA -> SG (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 714 714 A -> D (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 738 739 AV -> GW (in Ref. 7; AAB03088).
{ECO:0000305}.
CONFLICT 751 752 CV -> SL (in Ref. 10; AAB40654).
{ECO:0000305}.
CONFLICT 766 766 L -> S (in Ref. 9; AAB63202).
{ECO:0000305}.
CONFLICT 785 785 R -> K (in Ref. 9; AAB63202).
{ECO:0000305}.
CONFLICT 794 794 Y -> N (in Ref. 9; AAB63202).
{ECO:0000305}.
CONFLICT 846 846 I -> V (in Ref. 9; AAB63201).
{ECO:0000305}.
SEQUENCE 1162 AA; 130833 MW; BA7AC2CA2D2E62AF CRC64;
MTCQKFYVVL LHWEFLYVIT ALNLAYPTSP WRFKLFCAPP STTDDSFLSP AGVPNNTSSL
KGASEALVEA KFNSTGIYVS ELSKTIFHCC FGNEQGQNCS ALTGNTEGKT LASVVKPLVF
RQLGVNWDIE CWMKGDLTLF ICHMEPLLKN PFKNYDSKVH LLYDLPEVID DLPLPPLKDS
FQTVQCNCSV RECECHVPVP RAKVNYALLM YLEITSAGVS FQSPLMSLQP MLVVKPDPPL
GLRMEVTDDG NLKISWDSQT KAPFPLQYQV KYLENSTIVR EAAEIVSDTS LLVDSVLPGS
SYEVQVRSKR LDGSGVWSDW SLPQLFTTQD VMYFPPKILT SVGSNASFCC IYKNENQTIS
SKQIVWWMNL AEKIPETQYN TVSDHISKVT FSNLKATRPR GKFTYDAVYC CNEQACHHRY
AELYVIDVNI NISCETDGYL TKMTCRWSPS TIQSLVGSTV QLRYHRRSLY CPDNPSIRPT
SELKNCVLQT DGFYECVFQP IFLLSGYTMW IRINHSLGSL DSPPTCVLPD SVVKPLPPSN
VKAEITINTG LLKVSWEKPV FPENNLQFQI RYGLNGKEIQ WKTHEVFDAK SKSASLPVSD
LCAVYVVQVR CRRLDGLGYW SNWSSPAYTL VMDVKVPMRG PEFWRIMDGD ITKKERNVTL
LWKPLMKNDS LCSVRRYVVK HRTAHNGTWS QDVGNQTNLT FLWAESAHTV TVLAINSIGA
SLVNFNLTFS WPMSKVNAVQ SLSAYPLSSS CVILSWTLSP NDYSLLYLVI EWKNLNDDDG
MKWLRIPSNV NKYYIHDNFI PIEKYQFSLY PVFMEGVGKP KIINGFTKDD IAKQQNDAGL
YVIVPIIISS CVLLLGTLLI SHQRMKKLFW DDVPNPKNCS WAQGLNFQKP ETFEHLFTKH
AESVIFGPLL LEPEPVSEEI SVDTAWKNKD EMVPAAMVSL LLTTPDSTRG SICISDQCNS
ANFSGAQSTQ GTCEDECQSQ PSVKYATLVS NVKTVETDEE QGAIHSSVSQ CIARKHSPLR
QSFSSNSWEI EAQAFFLLSD HPPNVISPQL SFSGLDELLE LEGNFPEENH GEKSVYYLGV
SSGNKRENDM LLTDEAGVLC PFPAHCLFSD IRILQESCSH FVENNLNLGT SGKNFVPYMP
QFQSCSTHSH KIIENKMCDL TV


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