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Podocalyxin (GCTM-2 antigen) (Gp200) (Podocalyxin-like protein 1) (PC) (PCLP-1)

 PODXL_HUMAN             Reviewed;         558 AA.
O00592; A6NHX8; Q52LZ7; Q53ER6;
13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 135.
RecName: Full=Podocalyxin;
AltName: Full=GCTM-2 antigen;
AltName: Full=Gp200;
AltName: Full=Podocalyxin-like protein 1;
Short=PC;
Short=PCLP-1;
Flags: Precursor;
Name=PODXL; Synonyms=PCLP, PCLP1;
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 2), AND VARIANT LEU-194.
PubMed=9188463; DOI=10.1074/jbc.272.25.15708;
Kershaw D.B., Beck S.G., Wharram B.L., Wiggins J.E., Goyal M.,
Thomas P.E., Wiggins R.C.;
"Molecular cloning and characterization of human podocalyxin-like
protein. Orthologous relationship to rabbit PCLP1 and rat
podocalyxin.";
J. Biol. Chem. 272:15708-15714(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ILE-358.
TISSUE=Heart;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-310 (ISOFORM 1).
Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J.,
Nakai K., Sugano S.;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 399-411 AND 445-372.
PubMed=12504081; DOI=10.1016/S0006-291X(02)02844-9;
Schopperle W.M., Kershaw D.B., DeWolf W.C.;
"Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is
podocalyxin.";
Biochem. Biophys. Res. Commun. 300:285-290(2003).
[9]
FUNCTION, INTERACTION WITH EZR, AND SUBCELLULAR LOCATION.
PubMed=17616675; DOI=10.1158/0008-5472.CAN-06-3575;
Sizemore S., Cicek M., Sizemore N., Ng K.P., Casey G.;
"Podocalyxin increases the aggressive phenotype of breast and prostate
cancer cells in vitro through its interaction with ezrin.";
Cancer Res. 67:6183-6191(2007).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18456258; DOI=10.1016/j.yexcr.2008.03.009;
Larrucea S., Butta N., Arias-Salgado E.G., Alonso-Martin S.,
Ayuso M.S., Parrilla R.;
"Expression of podocalyxin enhances the adherence, migration, and
intercellular communication of cells.";
Exp. Cell Res. 314:2004-2015(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND THR-556, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in the regulation of both adhesion and cell
morphology and cancer progression. Function as an anti-adhesive
molecule that maintains an open filtration pathway between
neighboring foot processes in the podocyte by charge repulsion.
Acts as a pro-adhesive molecule, enhancing the adherence of cells
to immobilized ligands, increasing the rate of migration and cell-
cell contacts in an integrin-dependent manner. Induces the
formation of apical actin-dependent microvilli. Involved in the
formation of a preapical plasma membrane subdomain to set up
inital epithelial polarization and the apical lumen formation
during renal tubulogenesis. Plays a role in cancer development and
aggressiveness by inducing cell migration and invasion through its
interaction with the actin-binding protein EZR. Affects EZR-
dependent signaling events, leading to increased activities of the
MAPK and PI3K pathways in cancer cells.
{ECO:0000269|PubMed:17616675, ECO:0000269|PubMed:18456258}.
-!- SUBUNIT: Monomer; when associated with the membrane raft.
Oligomer; when integrated in the apical membrane. Interacts (via
the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ
domains); the interaction is not detected in glomerular epithelium
cells, take place early in the secretory pathway and is necessary
for its apical membrane sorting. Found in a complex with EZR,
PODXL and SLC9A3R2. Associates with the actin cytoskeleton through
complex formation with EZR and SLC9A3R2. Interacts (via the C-
terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1
domain); interaction is detected in glomerular epithelium cells
(By similarity). Interacts with EZR. {ECO:0000250,
ECO:0000269|PubMed:17616675}.
-!- INTERACTION:
P46940:IQGAP1; NbExp=4; IntAct=EBI-6897823, EBI-297509;
-!- SUBCELLULAR LOCATION: Apical cell membrane. Cell projection,
lamellipodium. Cell projection, filopodium. Cell projection,
ruffle. Cell projection, microvillus {ECO:0000250}. Membrane raft
{ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane
protein {ECO:0000305}. Note=In single attached epithelial cells is
restricted to a preapical pole on the free plasma membrane whereas
other apical and basolateral proteins are not yet polarized.
Colocalizes with SLC9A3R2 at the apical plasma membrane during
epithelial polarization. Colocalizes with SLC9A3R1 at the trans-
Golgi network (transiently) and at the apical plasma membrane. Its
association with the membrane raft is transient. Colocalizes with
actin filaments, EZR and SLC9A3R1 in a punctate pattern at the
apical cell surface where microvilli form. Colocalizes with EZR
and SLC9A3R2 at the apical cell membrane of glomerular epithelium
cells (By similarity). Forms granular, punctuated pattern, forming
patches, preferentially adopting a polar distribution, located on
the migrating poles of the cell or forming clusters along the
terminal ends of filipodia establishing contact with the
endothelial cells. Colocalizes with the submembrane actin of
lamellipodia, particularly associated with ruffles. Colocalizes
with vinculin at protrusions of cells. Colocalizes with ITGB1.
Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in
apical membrane initiation sites (AMIS) during the generation of
apical surface and luminogenesis (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00592-1; Sequence=Displayed;
Name=2;
IsoId=O00592-2; Sequence=VSP_037220;
-!- TISSUE SPECIFICITY: Glomerular epithelium cell (podocyte).
-!- DOMAIN: Both the O-glycan-rich domain of the extracellular domain
and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic
tail harbor an apical sorting signal. The cytoplasmic domain is
necessary for the apical membrane targeting and renal
tubulogenesis. The cytoplasmic C-terminus PDZ-binding motif (DTHL)
is essential for interaction with SLC9A3R1 and for targeting
SLC9A3R1 to the apical cell membrane. The extracellular domain is
necessary for microvillus formation (By similarity). The large
highly anionic extracellular domain allows to maintain open
filtration pathways between neighboring podocyte foot processes.
{ECO:0000250}.
-!- PTM: N- and O-linked glycosylated. Sialoglycoprotein (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the podocalyxin family. {ECO:0000305}.
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EMBL; U97519; AAB61574.1; -; mRNA.
EMBL; AK223573; BAD97293.1; -; mRNA.
EMBL; AC008264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236950; EAL24080.1; -; Genomic_DNA.
EMBL; CH471070; EAW83786.1; -; Genomic_DNA.
EMBL; BC093730; AAH93730.1; -; mRNA.
EMBL; BC112035; AAI12036.1; -; mRNA.
EMBL; BP234810; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS34755.1; -. [O00592-1]
CCDS; CCDS47714.1; -. [O00592-2]
RefSeq; NP_001018121.1; NM_001018111.2. [O00592-1]
RefSeq; NP_005388.2; NM_005397.3. [O00592-2]
UniGene; Hs.744213; -.
ProteinModelPortal; O00592; -.
SMR; O00592; -.
BioGrid; 111416; 22.
CORUM; O00592; -.
DIP; DIP-58638N; -.
IntAct; O00592; 7.
MINT; MINT-5000334; -.
STRING; 9606.ENSP00000367817; -.
iPTMnet; O00592; -.
PhosphoSitePlus; O00592; -.
SwissPalm; O00592; -.
BioMuta; PODXL; -.
EPD; O00592; -.
MaxQB; O00592; -.
PaxDb; O00592; -.
PeptideAtlas; O00592; -.
PRIDE; O00592; -.
Ensembl; ENST00000322985; ENSP00000319782; ENSG00000128567. [O00592-2]
Ensembl; ENST00000378555; ENSP00000367817; ENSG00000128567. [O00592-1]
GeneID; 5420; -.
KEGG; hsa:5420; -.
UCSC; uc003vqw.5; human. [O00592-1]
CTD; 5420; -.
DisGeNET; 5420; -.
EuPathDB; HostDB:ENSG00000128567.16; -.
GeneCards; PODXL; -.
H-InvDB; HIX0007089; -.
HGNC; HGNC:9171; PODXL.
HPA; CAB016169; -.
HPA; CAB062558; -.
HPA; CAB068219; -.
HPA; CAB068220; -.
HPA; HPA002110; -.
HPA; HPA045507; -.
MalaCards; PODXL; -.
MIM; 602632; gene.
neXtProt; NX_O00592; -.
OpenTargets; ENSG00000128567; -.
PharmGKB; PA33493; -.
eggNOG; ENOG410IFKB; Eukaryota.
eggNOG; ENOG410YCG4; LUCA.
GeneTree; ENSGT00730000111314; -.
HOVERGEN; HBG053629; -.
InParanoid; O00592; -.
KO; K06817; -.
OMA; QDECSIR; -.
OrthoDB; EOG091G0RL9; -.
PhylomeDB; O00592; -.
TreeFam; TF333564; -.
SIGNOR; O00592; -.
ChiTaRS; PODXL; human.
GeneWiki; PODXL; -.
GenomeRNAi; 5420; -.
PRO; PR:O00592; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128567; -.
CleanEx; HS_PODXL; -.
ExpressionAtlas; O00592; baseline and differential.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0036057; C:slit diaphragm; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0072175; P:epithelial tube formation; ISS:UniProtKB.
GO; GO:0072015; P:glomerular visceral epithelial cell development; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0032534; P:regulation of microvillus assembly; ISS:UniProtKB.
InterPro; IPR013836; CD34/Podocalyxin.
InterPro; IPR017403; PODXL.
PANTHER; PTHR12067; PTHR12067; 1.
Pfam; PF06365; CD34_antigen; 1.
PIRSF; PIRSF038143; Podocalyxin-like_p1; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 558 Podocalyxin.
/FTId=PRO_0000024754.
TOPO_DOM 23 461 Extracellular. {ECO:0000255}.
TRANSMEM 462 482 Helical. {ECO:0000255}.
TOPO_DOM 483 558 Cytoplasmic. {ECO:0000255}.
COMPBIAS 35 334 Thr-rich.
MOD_RES 518 518 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R0M4}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 537 537 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 556 556 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 360 360 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 236 268 LETVFHHVSQAGLELLTSGDLPTLASQSAGITA -> P
(in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9188463,
ECO:0000303|Ref.2}.
/FTId=VSP_037220.
VARIANT 60 60 T -> R.
/FTId=VAR_012236.
VARIANT 112 112 G -> S (in dbSNP:rs3735035).
/FTId=VAR_055237.
VARIANT 126 126 T -> P (in dbSNP:rs55698400).
/FTId=VAR_062136.
VARIANT 194 194 S -> L (in dbSNP:rs12670788).
{ECO:0000269|PubMed:9188463}.
/FTId=VAR_012237.
VARIANT 298 298 P -> A (in dbSNP:rs35893129).
/FTId=VAR_060090.
VARIANT 358 358 V -> I (in dbSNP:rs3212298).
{ECO:0000269|Ref.2}.
/FTId=VAR_055238.
CONFLICT 31 31 S -> SPS (in Ref. 1; AAB61574).
{ECO:0000305}.
CONFLICT 404 404 G -> Q (in Ref. 8; AA sequence).
{ECO:0000305}.
SEQUENCE 558 AA; 58635 MW; 8B1CF30D14D51691 CRC64;
MRCALALSAL LLLLSTPPLL PSSPSPSPSP SQNATQTTTD SSNKTAPTPA SSVTIMATDT
AQQSTVPTSK ANEILASVKA TTLGVSSDSP GTTTLAQQVS GPVNTTVARG GGSGNPTTTI
ESPKSTKSAD TTTVATSTAT AKPNTTSSQN GAEDTTNSGG KSSHSVTTDL TSTKAEHLTT
PHPTSPLSPR QPTSTHPVAT PTSSGHDHLM KISSSSSTVA IPGYTFTSPG MTTTLLETVF
HHVSQAGLEL LTSGDLPTLA SQSAGITASS VISQRTQQTS SQMPASSTAP SSQETVQPTS
PATALRTPTL PETMSSSPTA ASTTHRYPKT PSPTVAHESN WAKCEDLETQ TQSEKQLVLN
LTGNTLCAGG ASDEKLISLI CRAVKATFNP AQDKCGIRLA SVPGSQTVVV KEITIHTKLP
AKDVYERLKD KWDELKEAGV SDMKLGDQGP PEEAEDRFSM PLIITIVCMA SFLLLVAALY
GCCHQRLSQR KDQQRLTEEL QTVENGYHDN PTLEVMETSS EMQEKKVVSL NGELGDSWIV
PLDNLTKDDL DEEEDTHL


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U0768c CLIA Chicken,Gallus gallus,MEP21,PC,PCLP,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL,Thrombomucin 96T
E0768r ELISA kit PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl,Rat,Rattus norvegicus 96T
E0768m ELISA Mouse,Mus musculus,PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl 96T
E0768m ELISA kit Mouse,Mus musculus,PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl 96T
E0768r ELISA PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl,Rat,Rattus norvegicus 96T
U0768m CLIA Mouse,Mus musculus,PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl 96T
U0768r CLIA PC,Pclp1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,Podxl,Rat,Rattus norvegicus 96T
E0768Rb ELISA kit Oryctolagus cuniculus,PC,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL,Rabbit 96T
E0768Rb ELISA Oryctolagus cuniculus,PC,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL,Rabbit 96T
U0768Rb CLIA Oryctolagus cuniculus,PC,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL,Rabbit 96T
E0768c ELISA kit Canis familiaris,Canis lupus familiaris,cPCLP1,Dog,Gp135,PC,PC-like protein 1,PCLP,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL 96T
U0768c CLIA Canis familiaris,Canis lupus familiaris,cPCLP1,Dog,Gp135,PC,PC-like protein 1,PCLP,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL 96T
E0768c ELISA Canis familiaris,Canis lupus familiaris,cPCLP1,Dog,Gp135,PC,PC-like protein 1,PCLP,PCLP1,PCLP-1,Podocalyxin,Podocalyxin-like protein 1,PODXL 96T
1023 h Podocalyxin (human Podocalyxin ELISA, Strip Plate)
1023 Podocalyxin (h Podocalyxin ELISA, Strip Plate)
1033 r Podocalyxin (r Podocalyxin ELISA, Strip Plate)
1033 r Podocalyxin (rat Podocalyxin ELISA, Strip Plate)
1023.00 Podocalyxin (h Podocalyxin ELISA, Strip Plate) 1 kit


 

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