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Nephrin (Renal glomerulus-specific cell adhesion receptor)

 NPHN_MOUSE              Reviewed;        1256 AA.
Q9QZS7; D2KXA7; Q811S5; Q925S5; Q9ESC6; Q9ET59; Q9JIX1;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 2.
28-FEB-2018, entry version 147.
RecName: Full=Nephrin;
AltName: Full=Renal glomerulus-specific cell adhesion receptor;
Flags: Precursor;
Name=Nphs1; Synonyms=Nphn;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=10504499; DOI=10.1046/j.1523-1755.1999.00719.x;
Holzman L.B., St John P.L., Kovari I.A., Verma R., Holthoefer H.,
Abrahamson D.R.;
"Nephrin localizes to the slit pore of the glomerular epithelial
cell.";
Kidney Int. 56:1481-1491(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Kidney;
PubMed=10820162;
Putaala H., Sainio K., Sariola H., Tryggvason K.;
"Primary structure of mouse and rat nephrin cDNA and structure and
expression of the mouse gene.";
J. Am. Soc. Nephrol. 11:991-1001(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 1-494 (ISOFORM 1), FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=129/SvEv, and C57BL/6J;
PubMed=12039968; DOI=10.1074/jbc.M204806200;
Hamano Y., Grunkemeyer J.A., Sudhakar A., Zeisberg M., Cosgrove D.,
Morello R., Lee B., Sugimoto H., Kalluri R.;
"Determinants of vascular permeability in the kidney glomerulus.";
J. Biol. Chem. 277:31154-31162(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SELF-ASSOCIATION, INTERACTION
WITH KIRREL2, AND TISSUE SPECIFICITY.
PubMed=19887377; DOI=10.1074/jbc.M109.060657;
Nishida K., Hoshino M., Kawaguchi Y., Murakami F.;
"Ptf1a directly controls expression of immunoglobulin superfamily
molecules Nephrin and Neph3 in the developing central nervous
system.";
J. Biol. Chem. 285:373-380(2010).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 2), TISSUE
SPECIFICITY, AND ALTERNATIVE SPLICING.
STRAIN=129/Sv;
PubMed=12538735; DOI=10.1097/01.ASN.0000043081.65110.C4;
Beltcheva O., Kontusaari S., Fetissov S., Putaala H., Kilpelainen P.,
Hokfelt T., Tryggvason K.;
"Alternatively used promoters and distinct elements direct tissue-
specific expression of nephrin.";
J. Am. Soc. Nephrol. 14:352-358(2003).
[7]
INTERACTION WITH CD2AP.
PubMed=11733379; DOI=10.1016/S0002-9440(10)63080-5;
Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.;
"CD2AP localizes to the slit diaphragm and binds to nephrin via a
novel C-terminal domain.";
Am. J. Pathol. 159:2303-2308(2001).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=11136707; DOI=10.1093/hmg/10.1.1;
Putaala H., Soininen R., Kilpelainen P., Wartiovaara J.,
Tryggvason K.;
"The murine nephrin gene is specifically expressed in kidney, brain
and pancreas: inactivation of the gene leads to massive proteinuria
and neonatal death.";
Hum. Mol. Genet. 10:1-8(2001).
[9]
INTERACTION WITH CD2AP AND NPHS2.
PubMed=11733557; DOI=10.1172/JCI200112849;
Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W.,
Shaw A.S., Holzman L.B., Mundel P.;
"Podocin, a raft-associated component of the glomerular slit
diaphragm, interacts with CD2AP and nephrin.";
J. Clin. Invest. 108:1621-1629(2001).
[10]
INTERACTION WITH KIRREL1.
STRAIN=Swiss Webster; TISSUE=Brain;
PubMed=12424224; DOI=10.1096/fj.02-0242fje;
Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.;
"NEPH1 defines a novel family of podocin interacting proteins.";
FASEB J. 17:115-117(2003).
[11]
SELF-ASSOCIATION, AND INTERACTION WITH KIRREL1.
PubMed=12660326; DOI=10.1097/01.ASN.0000057853.05686.89;
Gerke P., Huber T.B., Sellin L., Benzing T., Walz G.;
"Homodimerization and heterodimerization of the glomerular podocyte
proteins nephrin and NEPH1.";
J. Am. Soc. Nephrol. 14:918-926(2003).
[12]
INTERACTION WITH KIRREL3.
PubMed=15843475; DOI=10.1681/ASN.2004060439;
Gerke P., Sellin L., Kretz O., Petraschka D., Zentgraf H., Benzing T.,
Walz G.;
"NEPH2 is located at the glomerular slit diaphragm, interacts with
nephrin and is cleaved from podocytes by metalloproteinases.";
J. Am. Soc. Nephrol. 16:1693-1702(2005).
[13]
INTERACTION WITH DDN.
PubMed=17537921; DOI=10.1073/pnas.0700917104;
Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
"Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
promotes apoptosis of podocytes.";
Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
[14]
INTERACTION WITH KIRREL3.
PubMed=18752272; DOI=10.1002/cne.21838;
Komori T., Gyobu H., Ueno H., Kitamura T., Senba E., Morikawa Y.;
"Expression of kin of irregular chiasm-like 3/mKirre in proprioceptive
neurons of the dorsal root ganglia and its interaction with nephrin in
muscle spindles.";
J. Comp. Neurol. 511:92-108(2008).
[15]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19470472; DOI=10.1073/pnas.0904398106;
Sohn R.L., Huang P., Kawahara G., Mitchell M., Guyon J., Kalluri R.,
Kunkel L.M., Gussoni E.;
"A role for nephrin, a renal protein, in vertebrate skeletal muscle
cell fusion.";
Proc. Natl. Acad. Sci. U.S.A. 106:9274-9279(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
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).
-!- FUNCTION: Seems to play a role in the development or function of
the kidney glomerular filtration barrier. Regulates glomerular
vascular permeability. May anchor the podocyte slit diaphragm to
the actin cytoskeleton. Plays a role in skeletal muscle formation
through regulation of myoblast fusion.
{ECO:0000269|PubMed:11136707, ECO:0000269|PubMed:12039968,
ECO:0000269|PubMed:19470472}.
-!- SUBUNIT: Interacts with NPHS2 and with CD2AP (via C-terminal
domain). Interacts with MAGI1 (via PDZ 2 and 3 domains) forming a
tripartite complex with IGSF5/JAM4. Forms a complex with ACTN4,
CASK, IQGAP1, MAGI2, SPTAN1 and SPTBN1 (By similarity). Interacts
with DDN; the interaction is direct. Self-associates (via the Ig-
like domains). Also interacts (via the Ig-like domains) with
KIRREL1 and KIRREL2; the interaction with KIRREL1 is dependent on
KIRREL1 glycosylation. Interacts with KIRREL3 (PubMed:15843475,
PubMed:18752272). {ECO:0000250|UniProtKB:Q9R044,
ECO:0000269|PubMed:11733379, ECO:0000269|PubMed:11733557,
ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:12660326,
ECO:0000269|PubMed:15843475, ECO:0000269|PubMed:17537921,
ECO:0000269|PubMed:18752272, ECO:0000269|PubMed:19887377}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}. Note=Located at podocyte
slit diaphragm between podocyte foot processes.
{ECO:0000269|PubMed:10504499}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=NephrinA;
IsoId=Q9QZS7-1; Sequence=Displayed;
Name=2; Synonyms=NephrinB;
IsoId=Q9QZS7-2; Sequence=VSP_040676;
-!- TISSUE SPECIFICITY: Expressed in kidney glomeruli. In the embryo,
expressed in the mesonephric kidney at E11 with strong expression
in cranial tubules with podocyte-like structures. Expression is
observed in the podocytes of the developing kidney from E13. High
expression is also detected in the developing cerebellum,
hindbrain, spinal cord, retina and hypothalamus. Expressed in
skeletal muscle during myoblast fusion such as in the adult
following acute injury and in the embryo but not detected in
uninjured adult skeletal muscle. Isoform 1 and isoform 2 are
expressed in the newborn brain and developing cerebellum. Isoform
1 is the predominant isoform in adult kidney.
{ECO:0000269|PubMed:10820162, ECO:0000269|PubMed:11136707,
ECO:0000269|PubMed:12538735, ECO:0000269|PubMed:19470472,
ECO:0000269|PubMed:19887377}.
-!- PTM: Phosphorylated at Tyr-1208 by FYN, leading to the recruitment
and activation of phospholipase C-gamma-1/PLCG1. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Death by postnatal day 2 associated with
proteinuria, edema and massive glomerular vascular leak. Kidneys
display enlarged Bowman's spaces, dilated tubuli, effacement of
podocyte foot processes and an absence of the glomerular
epithelial slit diaphragm. Impaired skeletal muscle development
characterized by incomplete myoblast fusion.
{ECO:0000269|PubMed:11136707, ECO:0000269|PubMed:12039968,
ECO:0000269|PubMed:19470472}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily.
{ECO:0000305}.
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EMBL; AF168466; AAF03368.1; -; mRNA.
EMBL; AF172254; AAF91085.1; -; Genomic_DNA.
EMBL; AF172247; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172248; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172249; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172250; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172251; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172252; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172253; AAF91085.1; JOINED; Genomic_DNA.
EMBL; AF172256; AAF91087.1; -; mRNA.
EMBL; AF190638; AAG17142.1; -; Genomic_DNA.
EMBL; AF191090; AAK38483.1; -; mRNA.
EMBL; AB513652; BAI63574.1; -; mRNA.
EMBL; AC167970; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY183460; AAO22850.1; -; Genomic_DNA.
CCDS; CCDS39884.1; -. [Q9QZS7-1]
RefSeq; NP_062332.2; NM_019459.2. [Q9QZS7-1]
RefSeq; XP_011248949.1; XM_011250647.1. [Q9QZS7-2]
UniGene; Mm.437830; -.
ProteinModelPortal; Q9QZS7; -.
BioGrid; 207694; 2.
CORUM; Q9QZS7; -.
DIP; DIP-61265N; -.
IntAct; Q9QZS7; 3.
STRING; 10090.ENSMUSP00000006825; -.
iPTMnet; Q9QZS7; -.
PhosphoSitePlus; Q9QZS7; -.
PaxDb; Q9QZS7; -.
PRIDE; Q9QZS7; -.
DNASU; 54631; -.
Ensembl; ENSMUST00000006825; ENSMUSP00000006825; ENSMUSG00000006649. [Q9QZS7-1]
Ensembl; ENSMUST00000126297; ENSMUSP00000116500; ENSMUSG00000006649. [Q9QZS7-2]
GeneID; 54631; -.
KEGG; mmu:54631; -.
UCSC; uc009gem.1; mouse. [Q9QZS7-2]
UCSC; uc009gen.1; mouse. [Q9QZS7-1]
CTD; 4868; -.
MGI; MGI:1859637; Nphs1.
eggNOG; KOG3515; Eukaryota.
eggNOG; ENOG410XRJN; LUCA.
GeneTree; ENSGT00550000074545; -.
HOVERGEN; HBG031752; -.
InParanoid; Q9QZS7; -.
OMA; LYMDVLP; -.
OrthoDB; EOG091G00UN; -.
PhylomeDB; Q9QZS7; -.
TreeFam; TF327139; -.
Reactome; R-MMU-373753; Nephrin family interactions.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-8866376; Reelin signalling pathway.
PRO; PR:Q9QZS7; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000006649; -.
CleanEx; MM_NPHS1; -.
ExpressionAtlas; Q9QZS7; baseline and differential.
Genevisible; Q9QZS7; MM.
GO; GO:0042995; C:cell projection; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:MGI.
GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
GO; GO:0017022; F:myosin binding; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IGI:MGI.
GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
GO; GO:0072015; P:glomerular visceral epithelial cell development; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; IDA:MGI.
GO; GO:0007520; P:myoblast fusion; IMP:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:MGI.
GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
GO; GO:0044062; P:regulation of excretion; IMP:UniProtKB.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF08205; C2-set_2; 5.
Pfam; PF00041; fn3; 1.
SMART; SM00060; FN3; 1.
SMART; SM00409; IG; 8.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 9.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50835; IG_LIKE; 8.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Developmental protein; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Myogenesis; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 1256 Nephrin.
/FTId=PRO_0000015053.
TOPO_DOM 36 1078 Extracellular. {ECO:0000255}.
TRANSMEM 1079 1099 Helical. {ECO:0000255}.
TOPO_DOM 1100 1256 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 144 Ig-like C2-type 1.
DOMAIN 149 247 Ig-like C2-type 2.
DOMAIN 256 347 Ig-like C2-type 3.
DOMAIN 354 448 Ig-like C2-type 4.
DOMAIN 454 554 Ig-like C2-type 5.
DOMAIN 558 649 Ig-like C2-type 6.
DOMAIN 754 846 Ig-like C2-type 7.
DOMAIN 852 953 Ig-like C2-type 8.
DOMAIN 957 1051 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000250|UniProtKB:O60500}.
MOD_RES 1112 1112 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R044}.
MOD_RES 1115 1115 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R044}.
MOD_RES 1119 1119 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R044}.
MOD_RES 1208 1208 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:Q9R044}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 415 415 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 722 722 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 67 125 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 174 231 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 279 331 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 375 431 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 479 542 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 581 637 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 775 830 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 877 934 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 33 MGAKEATVRGPGASPVHRTCHLIPLLLAGMLTT -> MEKW
RAWDPQSIQRRKTAK (in isoform 2).
{ECO:0000303|PubMed:19887377}.
/FTId=VSP_040676.
CONFLICT 1 24 MGAKEATVRGPGASPVHRTCHLIP -> MALGTTLRAS
(in Ref. 1; AAF03368). {ECO:0000305}.
CONFLICT 6 6 A -> V (in Ref. 2; AAF91087).
{ECO:0000305}.
CONFLICT 21 21 H -> R (in Ref. 2; AAF91087).
{ECO:0000305}.
CONFLICT 43 43 S -> P (in Ref. 2; AAF91085, 3; AAG17142/
AAK38483 and 4; BAI63574). {ECO:0000305}.
CONFLICT 63 63 V -> I (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 140 140 S -> R (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 145 145 I -> V (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 148 148 S -> P (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 178 178 D -> G (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 763 763 T -> A (in Ref. 1; AAF03368).
{ECO:0000305}.
CONFLICT 996 996 S -> T (in Ref. 1; AAF03368 and 2;
AAF91087). {ECO:0000305}.
CONFLICT 1076 1076 L -> Q (in Ref. 1; AAF03368).
{ECO:0000305}.
SEQUENCE 1256 AA; 136336 MW; 339A670F2AF000A2 CRC64;
MGAKEATVRG PGASPVHRTC HLIPLLLAGM LTTGLAQSPV PTSAPRGFWA LSENLTVVEG
STVKLWCGVR APGSVVQWAK DGLLLGPNPK IPGFPRYSLE GDSAKGEFHL LIEACDLSDD
AEYECQVGRS ELGPELVSPS VILSILVSPK VLQLTPEAGS TVTWVAGQEY VVTCVSGDAK
PAPDIIFIQG GRTVEDVSSS VNEGSEEKLF FTEAEARVTP QSSDNGQLLV CEGSNPALAT
PIKASFTMNI LFPPGPPVID WPGLNEGHVR AGENLELPCI ARGGNPPATL QWLKNGKPVS
IAWGTEHAQA VAHSVLVMTV RPEDHGARLS CQSYNSVSAE TQERSITLQV TFPPSAVTIL
GSTSQSENKN VTLCCLTKSS RPRVLLRWWL GGRQLLPTDE TVMDGLHGGH ISMSNLTLLV
KREDNGLSLT CEAFSDAFSK ETFKKSLTLN VKYPAQKLWI EGPPEGQSIR TGTRVRLVCL
AIGGNPEPSL TWLKDSRPVN DPRQSQEPRR VQLGSVEKSG STFSRELVLI IGPPDNLAKF
SCKAGQLSAS TQLVVQFPPT NLTILANSSA LRPGDALNLT CVSISSNPPV NLSLDKEGER
LDDVAAKPQS APFKGSAASR SVFLRVSSRD HGHRVTCRAH SEALRETVSS FYRLNVLYPP
EFLGEQVRAV TVVEQGQALL PVSVSANPAP EAFNWTFRGY RLSPAGGPRH RILSGGALQL
WNVTRADDGF YQLHCQNSEG TAEALLKLDV HYAPTIRALK DPTEVNVGGS VDIVCTVDAN
PILPEMFSWE RLGEDEEELN LDDMEKMSKG STGRLRIRQA KLSQAGAYQC IVDNGVAPAA
RGLVRLVVRF APQVDHPTPL TKVAAAGDST SSATLHCRAR GVPNIDFTWT KNGVPLDLQD
PRYTEHKYHQ GVVHSSLLTI ANVSAAQDYA LFKCTATNAL GSDHTNIQLV SISRPDPPLG
LKVVSVSPHS VGLEWKPGFD GGLPQRFQIR YEALESPGFL YMDVLPAQAT TFTLTGLKPS
TRYRIWLLAS NALGDSGLTD KGIQVSITTP GLDQAPEDTD QPLPTEQPPG PPRLPLLPVL
FAVGGLLLLS NASCVGGLLW RRRLRRLAEE ISEKTEAGSE EDRIRNEYEE SQWTGDRDTR
SSTVSTAEVD PHYYSMRDFS PQLPPTLEEV SYRQAFTGIE DEDMAFPGHL YDEVERVYGP
PGVWGPLYDE VQMDPYDLRW PEVKYEDPRG IYDQVAADMD AGEPGSLPFE LRGHLV


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gen13319 NPHN_HUMAN Renal glomerulus-specific cell adhesion receptor ELISA tesk kit 1
gen13323 NPHN_MOUSE Renal glomerulus-specific cell adhesion receptor ELISA tesk kit 1
gen13327 NPHN_RAT Renal glomerulus-specific cell adhesion receptor ELISA tesk kit 1
2265 Kidney glomerulus-specific cell adhesion receptor 0.1 mg
2265 Kidney glomerulus-specific cell adhesion receptor 0.5 mg
AA0040 T-Cell Receptor Signaling Phospho-Specific Array includes 188 highly specific and well-characterized phosphorylation antibodies in the T-cell receptor signaling pathway. 2 Pieces/Box
5-81031 Human renal epithelial cell (normal), male, 53, renal cancer vial
MEDCLA319-1 Renal Cell Carcinoma Marker, Proximal Nephrogenic Renal Ag.,Carb. dom. of a 200kD gp200, Cl 66.4.C2,Mab anti_Hu; prfn 1 ml.
MEDCLA319-01 Renal Cell Carcinoma Marker, Proximal Nephrogenic Renal Ag.,Carb. dom. of a 200kD gp200, Cl 66.4.C2,Mab anti_Hu; prfn 0.1 ml.
20-783-73630 MOUSE ANTI HUMAN RENAL CELL CARCINOMA - Translocation-associated; Papillary renal cell carcinoma (Translocation-associated). isoform CRA_b Monoclonal 0.2 mg
EIAAB05126 Brain immunoglobulin receptor,CADM3,Cell adhesion molecule 3,Homo sapiens,Human,IgSF4B,IGSF4B,Immunoglobulin superfamily member 4B,NECL1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,
TS1068 Human renal clear cell carcinoma (90 cases) and normal renal (10 cases) Tissue Section 1 slide
TA1036 Human renal clear cell carcinoma (70 cases) and normal renal (10 cases) tissues array
TS1109 Human renal clear cell carcinoma (70 cases) and normal renal (10 cases) Tissue Section 1 slide
E1513m ELISA kit B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T
U1513m CLIA B-cell receptor CD22,BL-CAM,B-lymphocyte cell adhesion molecule,Cd22,Lyb-8,Mouse,Mus musculus,Sialic acid-binding Ig-like lectin 2,Siglec2,Siglec-2,T-cell surface antigen Leu-14 96T


 

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