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Mucin-4 (MUC-4) (Ascites sialoglycoprotein) (ASGP) (Pancreatic adenocarcinoma mucin) (Testis mucin) [Cleaved into: Mucin-4 alpha chain (Ascites sialoglycoprotein 1) (ASGP-1); Mucin-4 beta chain (Ascites sialoglycoprotein 2) (ASGP-2)]

 MUC4_MOUSE              Reviewed;        3443 AA.
Q8JZM8; Q4VAA3; Q9ERB8; Q9QXG0; Q9WV36;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
20-JUN-2018, entry version 90.
RecName: Full=Mucin-4;
Short=MUC-4;
AltName: Full=Ascites sialoglycoprotein;
Short=ASGP;
AltName: Full=Pancreatic adenocarcinoma mucin;
AltName: Full=Testis mucin;
Contains:
RecName: Full=Mucin-4 alpha chain;
AltName: Full=Ascites sialoglycoprotein 1;
Short=ASGP-1;
Contains:
RecName: Full=Mucin-4 beta chain;
AltName: Full=Ascites sialoglycoprotein 2;
Short=ASGP-2;
Flags: Precursor;
Name=Muc4;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=12084055; DOI=10.1046/j.1432-1033.2002.02988.x;
Desseyn J.-L., Clavereau I., Laine A.;
"Cloning, chromosomal localization and characterization of the murine
mucin gene orthologous to human MUC4.";
Eur. J. Biochem. 269:3150-3159(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-231.
STRAIN=CD-1;
Bartman A.E., Shekels L.L., Anway R.E., Gipson I.K., Moccia R.,
Ho S.B.;
"Identification and structure of a mouse homolog to the human MUC4
gene.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3076-3443.
STRAIN=FVB/N; TISSUE=Colon;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 3181-3351.
PubMed=12107190; DOI=10.1074/jbc.M206395200;
Lee C.G., Homer R.J., Cohn L., Link H., Jung S., Craft J.E.,
Graham B.S., Johnson T.R., Elias J.A.;
"Transgenic overexpression of interleukin (IL)-10 in the lung causes
mucus metaplasia, tissue inflammation, and airway remodeling via IL-
13-dependent and -independent pathways.";
J. Biol. Chem. 277:35466-35474(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3343-3443.
STRAIN=CF-1; TISSUE=Uterine horn luminal epithelium;
DeSouza M.M., Carson D.D., Harris M.N., Julian J.;
"Cloning and expression analysis of mouse ascites sialoglycoprotein-2
(ASGP-2)/Mucin 4 (Muc4).";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: May play a role in tumor progression. Ability to promote
tumor growth may be mainly due to repression of apoptosis as
opposed to proliferation. Has anti-adhesive properties. Seems to
alter cellular behavior through both anti-adhesive effects on
cell-cell and cell-extracellular matrix interactions and in its
ability to act as an intramembrane ligand for ERBB2. Plays an
important role in cell proliferation and differentiation of
epithelial cells by inducing specific phosphorylation of ERBB2.
The MUC4-ERBB2 complex causes site-specific phosphorylation of the
ERBB2 'Tyr-1248'. In polarized epithelial cells segregates ERBB2
and other ERBB receptors and prevents ERBB2 from acting as a
coreceptor. The interaction with ERBB2 leads to enhanced
expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1
complex leads to down-regulation of CDKN1B, resulting in
repression of apoptosis and stimulation of proliferation (By
similarity). {ECO:0000250}.
-!- SUBUNIT: A heterodimeric complex, composed of a mucin-4 alpha
chain and a cysteine-rich transmembrane mucin-4 beta chain. Mucin-
4 beta chain interacts with ERBB2 via the EGF-like domain 1. In
nonpolarized cells, associates with ERBB2 and ERBB3 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
Secreted. Note=Secreted by proteolytic processing. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in trachea, duodenum and intestine.
Lower expression in stomach, salivary glands, liver, gallbladder,
and kidney. {ECO:0000269|PubMed:12084055}.
-!- PTM: Proteolytically cleaved into 2 chains, mucin-4 alpha chain
and mucin-4 beta chain. {ECO:0000250}.
-!- PTM: Mucin-4 alpha chain is highly O-glycosylated.
-!- PTM: Mucin-4 beta chain is predominantly N-glycosylated.
{ECO:0000250}.
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EMBL; AF441786; AAM66254.1; -; mRNA.
EMBL; AF520422; AAM66746.1; -; Genomic_DNA.
EMBL; AF520421; AAM66746.1; JOINED; Genomic_DNA.
EMBL; AY007202; AAG02256.1; -; mRNA.
EMBL; BC096477; AAH96477.1; -; mRNA.
EMBL; AF218819; AAF25480.1; -; mRNA.
EMBL; AF161256; AAD43349.1; -; mRNA.
UniGene; Mm.214599; -.
ProteinModelPortal; Q8JZM8; -.
MaxQB; Q8JZM8; -.
PeptideAtlas; Q8JZM8; -.
PRIDE; Q8JZM8; -.
MGI; MGI:2153525; Muc4.
HOVERGEN; HBG081997; -.
InParanoid; Q8JZM8; -.
PhylomeDB; Q8JZM8; -.
ChiTaRS; Muc4; mouse.
PRO; PR:Q8JZM8; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MUC4; -.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031528; C:microvillus membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005176; F:ErbB-2 class receptor binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
GO; GO:0002853; P:negative regulation of T cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
InterPro; IPR005533; AMOP_dom.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR003886; NIDO_dom.
InterPro; IPR001846; VWF_type-D.
Pfam; PF06119; NIDO; 1.
Pfam; PF00094; VWD; 1.
SMART; SM00723; AMOP; 1.
SMART; SM00181; EGF; 3.
SMART; SM00539; NIDO; 1.
SMART; SM00216; VWD; 1.
PROSITE; PS50856; AMOP; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS51220; NIDO; 1.
PROSITE; PS51233; VWFD; 1.
2: Evidence at transcript level;
Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 3443 Mucin-4.
/FTId=PRO_0000274227.
CHAIN 29 2718 Mucin-4 alpha chain.
/FTId=PRO_0000274228.
CHAIN 2719 3443 Mucin-4 beta chain.
/FTId=PRO_0000274229.
TRANSMEM 3405 3425 Helical. {ECO:0000255}.
REPEAT 93 213 1.
REPEAT 333 454 2.
REPEAT 455 580 3.
REPEAT 581 685 4.
REPEAT 686 786 5.
REPEAT 787 994 6.
REPEAT 995 1273 7.
REPEAT 1274 1399 8.
REPEAT 1400 1525 9.
REPEAT 1526 1651 10.
REPEAT 1652 1775 11.
REPEAT 1776 1899 12.
REPEAT 1900 2025 13.
REPEAT 2026 2151 14.
DOMAIN 2431 2586 NIDO. {ECO:0000255|PROSITE-
ProRule:PRU00570}.
DOMAIN 2587 2699 AMOP. {ECO:0000255|PROSITE-
ProRule:PRU00347}.
DOMAIN 2712 2946 VWFD. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 3146 3185 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3355 3394 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 29 2338 Thr-rich.
COMPBIAS 37 2337 Ser-rich.
COMPBIAS 2773 3120 Ser/Thr-rich.
SITE 2718 2719 Cleavage.
CARBOHYD 98 98 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 385 385 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 465 465 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 517 517 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 550 550 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 627 627 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 756 756 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 793 793 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 797 797 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 833 833 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 907 907 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 920 920 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 964 964 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1046 1046 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1114 1114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1243 1243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1320 1320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1369 1369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1382 1382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1495 1495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1621 1621 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1745 1745 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1869 1869 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1995 1995 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2077 2077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2121 2121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2728 2728 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2746 2746 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2774 2774 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2800 2800 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2817 2817 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2826 2826 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2861 2861 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2882 2882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2889 2889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2905 2905 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2931 2931 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2958 2958 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2976 2976 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2987 2987 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3027 3027 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3052 3052 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3075 3075 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3082 3082 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3130 3130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3147 3147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3213 3213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3220 3220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3326 3326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3150 3161 {ECO:0000250}.
DISULFID 3155 3173 {ECO:0000250}.
DISULFID 3175 3184 {ECO:0000250}.
DISULFID 3358 3369 {ECO:0000250}.
DISULFID 3363 3378 {ECO:0000250}.
DISULFID 3380 3393 {ECO:0000250}.
CONFLICT 24 24 P -> PE (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 36 36 M -> V (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 139 139 S -> R (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 156 156 E -> D (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 203 203 R -> S (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 225 225 S -> L (in Ref. 2; AAG02256).
{ECO:0000305}.
CONFLICT 3094 3094 G -> A (in Ref. 3; AAH96477).
{ECO:0000305}.
CONFLICT 3162 3162 G -> D (in Ref. 3; AAH96477).
{ECO:0000305}.
CONFLICT 3180 3180 A -> T (in Ref. 3; AAH96477).
{ECO:0000305}.
CONFLICT 3181 3181 D -> G (in Ref. 4; AAF25480).
{ECO:0000305}.
CONFLICT 3197 3197 T -> M (in Ref. 4; AAF25480).
{ECO:0000305}.
CONFLICT 3205 3205 M -> V (in Ref. 3; AAH96477 and 4;
AAF25480). {ECO:0000305}.
CONFLICT 3225 3225 N -> Y (in Ref. 3; AAH96477).
{ECO:0000305}.
CONFLICT 3322 3322 Q -> K (in Ref. 3; AAH96477).
{ECO:0000305}.
CONFLICT 3384 3384 T -> I (in Ref. 3; AAH96477 and 5;
AAD43349). {ECO:0000305}.
CONFLICT 3391 3391 K -> E (in Ref. 3; AAH96477 and 5;
AAD43349). {ECO:0000305}.
CONFLICT 3432 3432 M -> K (in Ref. 3; AAH96477 and 5;
AAD43349). {ECO:0000305}.
SEQUENCE 3443 AA; 365216 MW; 88CC32D3226F632B CRC64;
MRGPHWRVPW LCLSCLYSCL LLLPDALATT STQTPMSLSS STRTSQMSSQ ASTSSTSSDR
RTSKTEQTST RDTPSSITTV SQSHHTTSME TSKPQTTTTT EVTTSTPSAS SRDQIQTETS
SQRTISPDGT TTSHAPSISS SAPSTTHMLT TTSSTESTSV DSGHTTAITT QGLTPATAQV
SLTPSSQNMS TVSTPITSTL TQRQHTGSKQ TSSKSQVNIV TSTLSTSTSD STPAQTMSQV
TSSSDKRTKP STSGVSSTSL TTTEVLTQTS STDSAPGNTT LRITQNSTTH TTKVSTTSTP
QKLSPVSTLI NSSQKMSTLP QNQHTESMDT SRQPQTTTTT EVTTSTPSAS SLHQIQTETN
SQKTISPGET TTSHAPNMRS SPPKTSQILT TMPSTKSTSV DTKQTKAITT KVSTPDTTQV
SMTPSSQKLP THSTSTQELT SSYSQHIQSK GTSSKSQTTT NTKVNTSTPS ASSRDKIQTE
TSSQRTNSPG EKRTSHGPSM SSSAPSTTHM LSTTSSNQST SVDTGQTTSV TAQGSTPAIT
QTSLTPSSQN MSTVSTPITS TQILSTLPQS QHTGSMGTSS NPQTTTSPVV TTSTPSGTSG
DQIQTETSSQ RTISPGKTTI SHAPNINSSA PSTTHMLSTT SSTQSTSGDT RHITAGRTQG
STPATTQTSL TPSSPXXXXX XXXXXETETS SQRTISPGET TTSHAPIMSS SPPSSTHMLS
TASSTEITSV DTRHTTAIMT QGSTPATTQV SPSSQNMSTV SAPITSTHIL STLSQSQHTG
SKGTSSNPQT TTTPVVTTST PSASSRDQIQ TETSSQRTIS PGKTTTSHVP NMNSSAPSTT
HILSTTSSIQ STSGDTRHTT AVRTQGSTPA TTQVSLTPSS QXXXXXXXXX XETETSSLRT
ISPDGTTTSH ASSMSSSSPN TTHLLFTTSS TESTSVDTGH STVITTHGST LATTQVSLTP
SSQNMSTVSA PITSSQILST LRQSQHTGSK GTSSNHQTTT TPVVTTSTPS AASRDQIQTE
TSSLRTISPD GTTTSHASSM SSSSPNTTHL LITTSSTEST SVDTGHSTVI TTHGSTLATT
XXXXXXXXXX ETETSSQRTI SPGKTTTSHV PNMNSSAPST THISSTTSSI QSTSGDTRHT
TAVRTQGSTP ATTQVSLTPS SQXXXXXXXX XXETETSSQR TISLGETTTS HAPIMSSSPP
SSTHMLSTAS STEITSVDTG HTTAIMTQGS TPATIQVSPS SQNMSTVSAP ITSTHILSTL
PKSQHTGSKG TSSNPQTTTT PVVTTSTPSA SSRDQIQTET SSQRTISPGK TTTSHVPNMN
SSAPSTTHIL STTSSTQSTS GDTRHTTAVR TQGPTPATTQ VSLAPSSQNM STLSAPITSP
QNFSTLPQNQ HTGSMGTSSN PQSTTIPEVT TSTLSASSRD QVQTETSSQR TIPPGETTTS
HASSLSSSGP STTNMLTRTS STQITSGDTR HTTAIVTQGS TPATTQTSLT PSSQNMSTVS
APITSSQILS TLRQSQHTGS KGTSSNHQTT TTPVVTTSTP SATSRDQIQT ETSSLRTISP
GETTTSHASS LSSSGPSTTN MLTRTSSTQI TSGDTRHTTA IVTQGSTPAT TQTSLTPSSR
NMSTVSTPIT STHKLSTLPQ RQHTGSKGTS SNPQTTTTPE MTTSTPSATS HDLIETETSS
QRTISPGETT TSYAPIMSSS APSTTHMLST TSSTRSTSVD TRHTTTLMTQ GSTPATTQVS
PSSKNMSTVS TPITSTHKLS TLPQSQHTGS KGTSSNPQTT TTPEVTTSTP SATTRDQIQT
ESSSQRTISP GETTTSHAPS MSSLAPSTTH MLSTTSSSQS TSGDTGHTTA VRTQGSTPAT
TQVSLSSQNI STVSTPMTST HKLSTLPQSQ HTGSMGTSSN PQTTTTPEVT TSTPSATSYD
QIQTETSFQR TISPGETTTS HAPSMSNSAP SSTHKLSTAS STEITSVDTR HTIAITTEGS
TLANTQTSLT PSSQNMSTVS APITSSQILS TLRQSQHTGS KGTSSNHQTT TTPVVTTSTP
SATSRDQIQT ETSSLRTISP DGTTTSHASS MSSSSPNTTH LLITTSSTES TSVDTGHSTV
ITTHGSTLAT TQVSLTPSSQ NMSTVSMPST SSQELTSLPQ RQHTGSMETS SQPQNITPTV
VTTSTLLSFS RGSTELQTMS WGTSSSGTIT TLSTPVRNTS PASTSGILTS TLTTSGNTGY
TGVTRSLGVI TSRVTSTSLP GKSTVVHSTP AQPLSAHSQS HQTYGTGTPS TSQISILPDV
TSEKHVASSP GPTVTESFSH VSSSSGLTTK TDNDRNTAVS ATSSTLTSPS PTTASRSTVP
LPSLLPDQGI SLFPYGSEVG DQNLFARTVD FNSPIFKILI GFPLGSSLRD SFYVTDNGQI
IFPESDYDVF SYPNPPQRGF TGRERVAMVA PFWADADFSS SRGAIFYQEY VTFYNGHHQL
IREVETLIND FTSSWGYRAK WTLKVTWVNV PAYTAQESFG TNTYQAILST DGSRSYALFL
YQNSGMRWDV TQEPYNRVLM GFSSGDGYFE NSPLTFRPAM EKYRPDRFLN SKLGIRGLQV
YRLHGEERPN YRLKCLRWLE SQPQQPSWGW SSVSCPCSWQ QGQRDFRFRP INPGWWDRQL
CSFSSGRGGV CCSYGAWGEF REGWRMHSPW QFDEEQEAQN WCCQWNDKPS FCVWYQLRRP
RVSCAGYRPP RPAWTFGDPH ITTLDNANFT FNGLGDFLLV QAQDRNSSFL LEGRTAQTGT
AKATNFIAFA AQYNTSSLKS PITVQWFLEP SDKIRVVYNN QTVAFNTRDT EVLPIFNTTG
VLLTQNGSQV SANFDGTVTI SVIARSNILH ASSSLSEEYR NHTEGLLGVW NDNPEDDFRM
PNGSTIPSNS SEETLFFYGM TWHVNGTGLL GIRADPLPTK FTPIFLSQLL NQSASGEDLA
SGCKGDRKCM FDILATGNRT IGQSTNSILN EFQHMNDTLN QYPPSINCSS KIQAYKGQTV
TTEITSNSKD ATLSLSKKCS GFQLFENGSL QWTPTSPEAC TLEILARDVR TNLSWVLQPK
TVACFCSKEE QCLYNETSKE GNSSLEVTSC KCDGDTFGRL CERFKDPCDE PCFPNVNCIP
GKGCEACPPN TTGDGRHCAA LEDSCPNRSC PVNYCYNNGH CGISEAPGCQ PTCTCPPAFA
DNRCFLAGNS FTPTISTELP LRTIMLSLRE DENASAADVN ASVANILENL DMRAFFSNSL
VELIRTSPGA QPSSKSIHHW KVTSHFKYRP RGPLIHYLNN QLIGAVMEAF LLQARQERQK
RSGEARKDVH FFPISRADVQ DQMALNLSML EEYFTCDGYK GYHLVYSPQD GVTCVSPCSE
GYCHNGGQCK HLPDGPQCSC ASFTIYTSSG KHCEHLSVKL GAFYGILFGT LGALLLLGIL
AFMIFHFCGC SMNKFSYPLD SEL


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U1034m CLIA Ascites sialoglycoprotein,ASGP,Mouse,Muc4,MUC-4,Mucin-4,Mus musculus,Pancreatic adenocarcinoma mucin,Testis mucin 96T
E1034r ELISA Ascites sialoglycoprotein,ASGP,Muc4,MUC-4,Mucin-4,Pancreatic adenocarcinoma mucin,Pre-sialomucin complex,pSMC,Rat,Rattus norvegicus,Sialomucin complex,Smc,Testis mucin 96T
E1034r ELISA kit Ascites sialoglycoprotein,ASGP,Muc4,MUC-4,Mucin-4,Pancreatic adenocarcinoma mucin,Pre-sialomucin complex,pSMC,Rat,Rattus norvegicus,Sialomucin complex,Smc,Testis mucin 96T
U1034r CLIA Ascites sialoglycoprotein,ASGP,Muc4,MUC-4,Mucin-4,Pancreatic adenocarcinoma mucin,Pre-sialomucin complex,pSMC,Rat,Rattus norvegicus,Sialomucin complex,Smc,Testis mucin 96T
E0684h ELISA Cervical mucin,High molecular weight salivary mucin MG1,Homo sapiens,Human,MUC5,MUC5B,MUC-5B,Mucin-5 subtype B, tracheobronchial,Mucin-5B,Sublingual gland mucin 96T
E0684h ELISA kit Cervical mucin,High molecular weight salivary mucin MG1,Homo sapiens,Human,MUC5,MUC5B,MUC-5B,Mucin-5 subtype B, tracheobronchial,Mucin-5B,Sublingual gland mucin 96T
U0684h CLIA Cervical mucin,High molecular weight salivary mucin MG1,Homo sapiens,Human,MUC5,MUC5B,MUC-5B,Mucin-5 subtype B, tracheobronchial,Mucin-5B,Sublingual gland mucin 96T
20-783-72954 MOUSE ANTI HUMAN MUCIN 5AC - MUC-5AC; Mucin-5 subtype AC. tracheobronchial; Tracheobronchial mucin; TBM; Major airway glycoprotein; Gastric mucin; Lewis B blood group antigen; LeB Monoclonal 0.2 mg
U0756h CLIA Gastric mucin,Homo sapiens,Human,LeB,Lewis B blood group antigen,Major airway glycoprotein,MUC5,MUC5AC,MUC-5AC,Mucin-5 subtype AC, tracheobronchial,Mucin-5AC,TBM,Tracheobronchial mucin 96T
E0756h ELISA Gastric mucin,Homo sapiens,Human,LeB,Lewis B blood group antigen,Major airway glycoprotein,MUC5,MUC5AC,MUC-5AC,Mucin-5 subtype AC, tracheobronchial,Mucin-5AC,TBM,Tracheobronchial mucin 96T
E0413h ELISA Breast carcinoma-associated antigen DF3,Carcinoma-associated mucin,EMA,Episialin,H23AG,Homo sapiens,Human,MUC1,MUC-1,Mucin-1,Peanut-reactive urinary mucin,PEM,PEMT,Polymorphic epithelial mucin,P 96T
U0413h CLIA Breast carcinoma-associated antigen DF3,Carcinoma-associated mucin,EMA,Episialin,H23AG,Homo sapiens,Human,MUC1,MUC-1,Mucin-1,Peanut-reactive urinary mucin,PEM,PEMT,Polymorphic epithelial mucin,PU 96T
E0756h ELISA kit Gastric mucin,Homo sapiens,Human,LeB,Lewis B blood group antigen,Major airway glycoprotein,MUC5,MUC5AC,MUC-5AC,Mucin-5 subtype AC, tracheobronchial,Mucin-5AC,TBM,Tracheobronchial mucin 96T
15-288-22681 Mucin-1 - MUC-1; Polymorphic epithelial mucin; PEM; PEMT; Episialin; Tumor-associated mucin; Carcinoma-associated mucin; Tumor-associated epithelial membrane antigen; EMA; H23AG; Peanut-reactive urina 0.1 mg
15-288-22681 Mucin-1 - MUC-1; Polymorphic epithelial mucin; PEM; PEMT; Episialin; Tumor-associated mucin; Carcinoma-associated mucin; Tumor-associated epithelial membrane antigen; EMA; H23AG; Peanut-reactive urina 0.05 mg
18-003-43701 Mucin-1 - MUC-1; Polymorphic epithelial mucin; PEM; PEMT; Episialin; Tumor-associated mucin; Carcinoma-associated mucin; Tumor-associated epithelial membrane antigen; EMA; H23AG; Peanut-reactive urina 0.1 mg Protein A
E0705m ELISA Colonic mucin,MCM,Mouse,Muc2,MUC-2,Mucin-2,Mus musculus,Secreted gel-forming mucin 96T
E0705m ELISA kit Colonic mucin,MCM,Mouse,Muc2,MUC-2,Mucin-2,Mus musculus,Secreted gel-forming mucin 96T
U0705m CLIA Colonic mucin,MCM,Mouse,Muc2,MUC-2,Mucin-2,Mus musculus,Secreted gel-forming mucin 96T
EIAAB25816 Gastric mucin-6,Mouse,Muc6,MUC-6,Mucin-6,Mus musculus,Secreted gel-forming mucin-6


 

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