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Peroxidasin homolog (EC 1.11.1.7) (Melanoma-associated antigen MG50) (Vascular peroxidase 1) (p53-responsive gene 2 protein)

 PXDN_HUMAN              Reviewed;        1479 AA.
Q92626; A8QM65; D6W4Y0; Q4KMG2;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
05-DEC-2018, entry version 173.
RecName: Full=Peroxidasin homolog;
EC=1.11.1.7;
AltName: Full=Melanoma-associated antigen MG50;
AltName: Full=Vascular peroxidase 1;
AltName: Full=p53-responsive gene 2 protein;
Flags: Precursor;
Name=PXDN; Synonyms=KIAA0230, MG50, PRG2, VPO, VPO1;
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 1), INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=10441517; DOI=10.1006/bbrc.1999.1123;
Horikoshi N., Cong J., Kley N., Shenk T.;
"Isolation of differentially expressed cDNAs from p53-dependent
apoptotic cells: activation of the human homologue of the Drosophila
peroxidasin gene.";
Biochem. Biophys. Res. Commun. 261:864-869(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=11103812;
Mitchell M.S., Kan-Mitchell J., Minev B., Edman C., Deans R.J.;
"A novel melanoma gene (MG50) encoding the interleukin 1 receptor
antagonist and six epitopes recognized by human cytolytic T
lymphocytes.";
Cancer Res. 60:6448-6456(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 3D-STRUCTURE MODELING,
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HEME
COFACTOR, AND TISSUE SPECIFICITY.
PubMed=18929642; DOI=10.1016/j.freeradbiomed.2008.09.009;
Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.;
"Identification and characterization of VPO1, a new animal heme-
containing peroxidase.";
Free Radic. Biol. Med. 45:1682-1694(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1479 (ISOFORM 2).
TISSUE=Chondrosarcoma;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1176 AND SER-1180, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[8]
SUBCELLULAR LOCATION.
Cheng G.;
Unpublished observations (FEB-2008).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION BY TGFB1.
PubMed=19590037; DOI=10.2353/ajpath.2009.080693;
Peterfi Z., Donko A., Orient A., Sum A., Prokai A., Molnar B.,
Vereb Z., Rajnavolgyi E., Kovacs K.J., Muller V., Szabo A.J.,
Geiszt M.;
"Peroxidasin is secreted and incorporated into the extracellular
matrix of myofibroblasts and fibrotic kidney.";
Am. J. Pathol. 175:725-735(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1178.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
INVOLVEMENT IN ASGD7, AND VARIANT ASGD7 CYS-880.
PubMed=21907015; DOI=10.1016/j.ajhg.2011.08.005;
Khan K., Rudkin A., Parry D.A., Burdon K.P., McKibbin M., Logan C.V.,
Abdelhamed Z.I., Muecke J.S., Fernandez-Fuentes N., Laurie K.J.,
Shires M., Fogarty R., Carr I.M., Poulter J.A., Morgan J.E.,
Mohamed M.D., Jafri H., Raashid Y., Meng N., Piseth H., Toomes C.,
Casson R.J., Taylor G.R., Hammerton M., Sheridan E., Johnson C.A.,
Inglehearn C.F., Craig J.E., Ali M.;
"Homozygous mutations in PXDN cause congenital cataract, corneal
opacity, and developmental glaucoma.";
Am. J. Hum. Genet. 89:464-473(2011).
-!- FUNCTION: Displays low peroxidase activity and is likely to
participate in H(2)O(2) metabolism and peroxidative reactions in
the cardiovascular system. Plays a role in extracellular matrix
formation. {ECO:0000269|PubMed:18929642,
ECO:0000269|PubMed:19590037}.
-!- CATALYTIC ACTIVITY:
Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor +
2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377,
ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521;
EC=1.11.1.7; Evidence={ECO:0000269|PubMed:18929642,
ECO:0000269|PubMed:19590037};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently
per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.15 mM for H(2)O(2) {ECO:0000269|PubMed:18929642};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:19590037, ECO:0000269|Ref.8}.
Note=Enriched in the peritubular space of fibrotic kidneys.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q92626-1; Sequence=Displayed;
Name=2;
IsoId=Q92626-2; Sequence=VSP_031516, VSP_031517;
-!- TISSUE SPECIFICITY: Expressed at higher levels in heart, lung,
ovary, spleen, intestine and placenta, and at lower levels in
liver, colon, pancreas, kidney, thymus, skeletal muscle and
prostate. Expressed in tumors such as melanoma, breast cancer,
ovarian cancer and glioblastoma. A shorter form probably lacking
the signal sequence is found in testis and in EB1 cells undergoing
p53/TP53-dependent apoptosis. {ECO:0000269|PubMed:10441517,
ECO:0000269|PubMed:11103812, ECO:0000269|PubMed:18929642,
ECO:0000269|PubMed:19590037}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal liver and spleen.
{ECO:0000269|PubMed:11103812}.
-!- INDUCTION: By TGFB1 in fibroblasts and up-regulated in apoptotic
cells. {ECO:0000269|PubMed:10441517, ECO:0000269|PubMed:19590037}.
-!- DISEASE: Anterior segment dysgenesis 7 (ASGD7) [MIM:269400]: A
form of anterior segment dysgenesis, a group of defects affecting
anterior structures of the eye including cornea, iris, lens,
trabecular meshwork, and Schlemm canal. Anterior segment
dysgeneses result from abnormal migration or differentiation of
the neural crest derived mesenchymal cells that give rise to
components of the anterior chamber during eye development.
Different anterior segment anomalies may exist alone or in
combination, including iris hypoplasia, enlarged or reduced
corneal diameter, corneal vascularization and opacity, posterior
embryotoxon, corectopia, polycoria, abnormal iridocorneal angle,
ectopia lentis, and anterior synechiae between the iris and
posterior corneal surface. Clinical conditions falling within the
phenotypic spectrum of anterior segment dysgeneses include
aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters
anomaly, and iridogoniodysgenesis. ASGD7 is an autosomal recessive
disease. {ECO:0000269|PubMed:21907015}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
-!- SEQUENCE CAUTION:
Sequence=AAF06354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA13219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF200348; AAF06354.1; ALT_INIT; mRNA.
EMBL; EF090903; ABO25865.1; -; mRNA.
EMBL; D86983; BAA13219.1; ALT_INIT; mRNA.
EMBL; CH471053; EAX01084.1; -; Genomic_DNA.
EMBL; CH471053; EAX01085.1; -; Genomic_DNA.
EMBL; BC098579; AAH98579.1; -; mRNA.
CCDS; CCDS46221.1; -. [Q92626-1]
RefSeq; NP_036425.1; NM_012293.2. [Q92626-1]
UniGene; Hs.332197; -.
ProteinModelPortal; Q92626; -.
SMR; Q92626; -.
BioGrid; 113596; 33.
IntAct; Q92626; 1.
STRING; 9606.ENSP00000252804; -.
PeroxiBase; 3355; HsPxd01.
GlyConnect; 1600; -.
iPTMnet; Q92626; -.
PhosphoSitePlus; Q92626; -.
SwissPalm; Q92626; -.
BioMuta; PXDN; -.
DMDM; 172045828; -.
EPD; Q92626; -.
MaxQB; Q92626; -.
PaxDb; Q92626; -.
PeptideAtlas; Q92626; -.
PRIDE; Q92626; -.
ProteomicsDB; 75381; -.
ProteomicsDB; 75382; -. [Q92626-2]
DNASU; 7837; -.
Ensembl; ENST00000252804; ENSP00000252804; ENSG00000130508. [Q92626-1]
GeneID; 7837; -.
KEGG; hsa:7837; -.
UCSC; uc002qxa.4; human. [Q92626-1]
CTD; 7837; -.
DisGeNET; 7837; -.
EuPathDB; HostDB:ENSG00000130508.10; -.
GeneCards; PXDN; -.
HGNC; HGNC:14966; PXDN.
HPA; HPA012375; -.
MalaCards; PXDN; -.
MIM; 269400; phenotype.
MIM; 605158; gene.
neXtProt; NX_Q92626; -.
OpenTargets; ENSG00000130508; -.
Orphanet; 289499; Congenital cataract microcornea with corneal opacity.
PharmGKB; PA128394535; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00940000157666; -.
HOGENOM; HOG000016084; -.
HOVERGEN; HBG108312; -.
InParanoid; Q92626; -.
KO; K19511; -.
OMA; VDFPCEA; -.
OrthoDB; EOG091G0236; -.
PhylomeDB; Q92626; -.
TreeFam; TF314316; -.
BRENDA; 1.11.1.7; 2681.
Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
ChiTaRS; PXDN; human.
GeneWiki; PXDN; -.
GenomeRNAi; 7837; -.
PRO; PR:Q92626; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000130508; Expressed in 218 organ(s), highest expression level in lung.
CleanEx; HS_PRG2; -.
CleanEx; HS_PXDN; -.
ExpressionAtlas; Q92626; baseline and differential.
Genevisible; Q92626; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005152; F:interleukin-1 receptor antagonist activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; IDA:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd09826; peroxidasin_like; 1.
Gene3D; 1.10.640.10; -; 1.
Gene3D; 2.60.40.10; -; 4.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR034828; Peroxidasin.
InterPro; IPR034824; Peroxidasin_peroxidase.
InterPro; IPR001007; VWF_dom.
PANTHER; PTHR11475:SF75; PTHR11475:SF75; 3.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF07679; I-set; 4.
Pfam; PF13855; LRR_8; 1.
Pfam; PF00093; VWC; 1.
PRINTS; PR00457; ANPEROXIDASE.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 4.
SMART; SM00369; LRR_TYP; 5.
SMART; SM00082; LRRCT; 1.
SMART; SM00214; VWC; 1.
SUPFAM; SSF48113; SSF48113; 1.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 4.
PROSITE; PS51450; LRR; 5.
PROSITE; PS50292; PEROXIDASE_3; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Disease mutation;
Disulfide bond; Extracellular matrix; Glycoprotein; Heme;
Hydrogen peroxide; Immunoglobulin domain; Iron; Leucine-rich repeat;
Metal-binding; Oxidoreductase; Peroxidase; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1479 Peroxidasin homolog.
/FTId=PRO_0000319619.
DOMAIN 27 63 LRRNT.
REPEAT 87 108 LRR 1.
REPEAT 111 132 LRR 2.
REPEAT 135 156 LRR 3.
REPEAT 159 180 LRR 4.
DOMAIN 192 245 LRRCT.
DOMAIN 246 332 Ig-like C2-type 1.
DOMAIN 342 428 Ig-like C2-type 2.
DOMAIN 433 520 Ig-like C2-type 3.
DOMAIN 521 610 Ig-like C2-type 4.
DOMAIN 1413 1471 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
ACT_SITE 827 827 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 828 828 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 907 907 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 909 909 Calcium; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
METAL 911 911 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 913 913 Calcium. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
METAL 1074 1074 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 826 826 Heme (covalent; via 2 links).
{ECO:0000250}.
BINDING 980 980 Heme (covalent; via 2 links).
{ECO:0000250}.
SITE 977 977 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
MOD_RES 1176 1176 Phosphotyrosine.
{ECO:0000244|PubMed:18318008}.
MOD_RES 1180 1180 Phosphoserine.
{ECO:0000244|PubMed:18318008}.
CARBOHYD 640 640 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 699 699 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 719 719 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 731 731 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1178 1178 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1280 1280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1368 1368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1425 1425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 267 317 {ECO:0000250}.
DISULFID 363 412 {ECO:0000250}.
DISULFID 454 502 {ECO:0000250}.
DISULFID 546 594 {ECO:0000250}.
DISULFID 732 748 {ECO:0000250}.
DISULFID 847 857 {ECO:0000250}.
DISULFID 851 875 {ECO:0000250}.
DISULFID 959 970 {ECO:0000250}.
DISULFID 1177 1234 {ECO:0000250}.
DISULFID 1275 1301 {ECO:0000250}.
VAR_SEQ 703 727 YHYNDLVSPQYLNLIANLSGCTAHR -> QCQSLFFLLHGL
SNGVEHASVKSHS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031516.
VAR_SEQ 728 1479 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031517.
VARIANT 880 880 R -> C (in ASGD7; dbSNP:rs587777572).
{ECO:0000269|PubMed:21907015}.
/FTId=VAR_071389.
VARIANT 1198 1198 R -> Q (in dbSNP:rs6723697).
/FTId=VAR_050487.
VARIANT 1261 1261 Q -> R (in dbSNP:rs6723697).
/FTId=VAR_039048.
SEQUENCE 1479 AA; 165275 MW; 7A75F533D89C6AAD CRC64;
MAKRSRGPGR RCLLALVLFC AWGTLAVVAQ KPGAGCPSRC LCFRTTVRCM HLLLEAVPAV
APQTSILDLR FNRIREIQPG AFRRLRNLNT LLLNNNQIKR IPSGAFEDLE NLKYLYLYKN
EIQSIDRQAF KGLASLEQLY LHFNQIETLD PDSFQHLPKL ERLFLHNNRI THLVPGTFNH
LESMKRLRLD SNTLHCDCEI LWLADLLKTY AESGNAQAAA ICEYPRRIQG RSVATITPEE
LNCERPRITS EPQDADVTSG NTVYFTCRAE GNPKPEIIWL RNNNELSMKT DSRLNLLDDG
TLMIQNTQET DQGIYQCMAK NVAGEVKTQE VTLRYFGSPA RPTFVIQPQN TEVLVGESVT
LECSATGHPP PRISWTRGDR TPLPVDPRVN ITPSGGLYIQ NVVQGDSGEY ACSATNNIDS
VHATAFIIVQ ALPQFTVTPQ DRVVIEGQTV DFQCEAKGNP PPVIAWTKGG SQLSVDRRHL
VLSSGTLRIS GVALHDQGQY ECQAVNIIGS QKVVAHLTVQ PRVTPVFASI PSDTTVEVGA
NVQLPCSSQG EPEPAITWNK DGVQVTESGK FHISPEGFLT INDVGPADAG RYECVARNTI
GSASVSMVLS VNVPDVSRNG DPFVATSIVE AIATVDRAIN STRTHLFDSR PRSPNDLLAL
FRYPRDPYTV EQARAGEIFE RTLQLIQEHV QHGLMVDLNG TSYHYNDLVS PQYLNLIANL
SGCTAHRRVN NCSDMCFHQK YRTHDGTCNN LQHPMWGASL TAFERLLKSV YENGFNTPRG
INPHRLYNGH ALPMPRLVST TLIGTETVTP DEQFTHMLMQ WGQFLDHDLD STVVALSQAR
FSDGQHCSNV CSNDPPCFSV MIPPNDSRAR SGARCMFFVR SSPVCGSGMT SLLMNSVYPR
EQINQLTSYI DASNVYGSTE HEARSIRDLA SHRGLLRQGI VQRSGKPLLP FATGPPTECM
RDENESPIPC FLAGDHRANE QLGLTSMHTL WFREHNRIAT ELLKLNPHWD GDTIYYETRK
IVGAEIQHIT YQHWLPKILG EVGMRTLGEY HGYDPGINAG IFNAFATAAF RFGHTLVNPL
LYRLDENFQP IAQDHLPLHK AFFSPFRIVN EGGIDPLLRG LFGVAGKMRV PSQLLNTELT
ERLFSMAHTV ALDLAAINIQ RGRDHGIPPY HDYRVYCNLS AAHTFEDLKN EIKNPEIREK
LKRLYGSTLN IDLFPALVVE DLVPGSRLGP TLMCLLSTQF KRLRDGDRLW YENPGVFSPA
QLTQIKQTSL ARILCDNADN ITRVQSDVFR VAEFPHGYGS CDEIPRVDLR VWQDCCEDCR
TRGQFNAFSY HFRGRRSLEF SYQEDKPTKK TRPRKIPSVG RQGEHLSNST SAFSTRSDAS
GTNDFREFVL EMQKTITDLR TQIKKLESRL STTECVDAGG ESHANNTKWK KDACTICECK
DGQVTCFVEA CPPATCAVPV NIPGACCPVC LQKRAEEKP


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CSB-EL011825MO Mouse Immune-responsive gene 1 protein homolog(IRG1) ELISA kit SpeciesMouse 96T
CSB-EL011825HU Human Immune-responsive gene 1 protein homolog(IRG1) ELISA kit SpeciesHuman 96T
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
15-288-21943 39S ribosomal protein L28. mitochondrial - L28mt; MRP-L28; Melanoma antigen p15; Melanoma-associated antigen recognized by T lymphocytes Polyclonal 0.1 mg
15-288-21943 39S ribosomal protein L28. mitochondrial - L28mt; MRP-L28; Melanoma antigen p15; Melanoma-associated antigen recognized by T lymphocytes Polyclonal 0.05 mg
10-288-21943F 39S ribosomal protein L28. mitochondrial - L28mt; MRP-L28; Melanoma antigen p15; Melanoma-associated antigen recognized by T lymphocytes 0.05 mg
10-288-21943F 39S ribosomal protein L28. mitochondrial - L28mt; MRP-L28; Melanoma antigen p15; Melanoma-associated antigen recognized by T lymphocytes 0.1 mg
EIAAB35258 39S ribosomal protein L28, mitochondrial,Homo sapiens,Human,L28mt,MAAT1,Melanoma antigen p15,Melanoma-associated antigen recognized by T lymphocytes,MRPL28,MRP-L28
EIAAB06373 CD63,CD63 antigen,Granulophysin,Homo sapiens,Human,LAMP-3,Lysosomal-associated membrane protein 3,Melanoma-associated antigen ME491,MLA1,Ocular melanoma-associated antigen,OMA81H,Tetraspanin-30,TSPAN3
PXDN PXDN Gene peroxidasin homolog (Drosophila)
PXDNL PXDNL Gene peroxidasin homolog (Drosophila)-like
EIAAB05142 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Mouse,Mus musculus
EIAAB05141 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Rat,Rattus norvegicus
EIAAB45312 14.5 kDa translational inhibitor protein,Heat-responsive protein 12,Homo sapiens,HRSP12,Human,p14.5,PSP,Ribonuclease UK114,UK114 antigen homolog
EIAAB39105 MAP-responsive gene protein,Methamphetamine-responsive transcript 1 protein,Mrt1,PDZ-protein Mrt1,Rat,Rattus norvegicus,Snx27,Sorting nexin-27
20-783-71555 MOUSE ANTI HUMAN CD63 FITC - Melanoma 1 antigen; CD63 antigen (Melanoma 1 antigen). isoform CRA_a; CD63 protein Monoclonal 0.1 mg
EIAAB09239 BBF2 human homolog on chromosome 7,BBF2H7,cAMP-responsive element-binding protein 3-like protein 2,CREB3L2,Cyclic AMP-responsive element-binding protein 3-like protein 2,Homo sapiens,Human
20-272-191634 CD146 (FITC) - Mouse monoclonal [2Q401] to CD146 (FITC); Melanoma-associated antigen MUC18; Melanoma cell adhesion molecule; Melanoma-associated antigen A32; S-endo 1 endothelial-associated antigen; C 0.025 mg


 

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