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ELISA Kit for Rat Mucin-4

SKU : BHE13806050

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1034r
Alternative Names	Ascites sialoglycoprotein ; ASGP ; Pancreatic adenocarcinoma mucin ; Pre-sialomucin complex ; pSMC ; Sialomucin complex ; Testis mucin ; Smc
Categories	Elisa
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. In polarized epithelilal cells segragates 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. The MUC4-ERBB2 complex causes site-specific phosphorylation of the ERBB2 'Tyr-1248'.
Specificity	Natural and recombinant Rat Mucin-4
Subcellular Location	Mucin-4 alpha chain Secreted Secreted by proteolytic processing.
Detection Range	0.156-10ng/mL
Entryname	MUC4_RAT
Method Type	Sandwich
Platform	PF06119
Protein Name	Mucin-4
Sensitivity	0.084ng/mL
Sequence	50: MRGPHGVSWR ; VPWLCLSCLC ; SCLLLLPVNT ; STTSAPKTST ; ALPSSTNPSQ ; 100: MTSQVSNPTA ; SSYRMTKNTG ; QASPMVTSSS ; ITTLPQSQHT ; GSMKTTRNPQ ; 150: TTGTTEVTTT ; LSASSSDQVQ ; VETTSQTTLS ; PDTTTTSHAP ; RESSSPPSTS ; 200: VILTTTASTE ; GTSGDTGHTM ; AVTTQGSTPA ; TTEISVTPST ; QKMSPVSTFS ; 250: TSTQEITTLS ; QSQHTGGMKT ; TRNPQTTGTT ; EVTTTLSASS ; SDHPTSSPES ; 300: TPGNTAPRTT ; ETSTTTTTKV ; LMTSLQQKLP ; TGSTLGTSTQ ; ELTTLPQSQH ; 350: TGIMKTTSRT ; QTTTPTEVTT ; RTLSASSSDH ; RQAETSSQTT ; LSPDTTTTSH ; 400: APRESSPPST ; SVILTHGHRE ; GTSGDTGHTM ; AVTTQGSTPA ; TTEISVTPST ; 450: QKMSPVSTFS ; TSTQEITTLS ; QSQHTGGMKT ; TRNPQRTTPT ; EVTTSTLSAS ; 500: SSDQVQVETT ; SRATLSPDTT ; TTSHAPSVSS ; SSPSPPSTEG ; TSVDTGLTTA ; 550: VTTQDSTPAT ; TQGSLTSSSQ ; TLSTVSPLST ; STQETSTQEL ; TSSQSQHTGS ; 600: MKTTHNPQTT ; RNTEVTTTLS ; ASSSDQVQVE ; TTSQTTLSDA ; TTTSHAPRES ; 650: SSPPSTSDIL ; TTMASTEGTS ; GDTGHTMAVT ; TQGSTPATTE ; ISVTPSTQKM ; 700: SPVSTFSTST ; QEITTLSQSQ ; HTGGMKTTRN ; PQTTGTTEVT ; TTLSASSSDQ ; 750: VQAETSSQTT ; LSPDTTTTSH ; APRESSSPPS ; TSDMLTTTAS ; TEGTSGDTGH ; 800: TTAVTTQGSI ; PATTQLSTTF ; ASQKMSTVST ; PTTSSIQELS ; TLPQSQHTGS ; 850: MEISSRPQTT ; SVTSTLSSSP ; SGSTPVQTRS ; VTSSSDERTN ; PTSSGVSNTS ; 900: PATTEVLTPT ; SSPESTPGNT ; APRTTETSTT ; TTTKVLMTSL ; QQKLPTGSTL ; 950: GTSTPTEVTT ; TLSASSSDQV ; QVETTSQTTL ; SPDATTTSHA ; PRESSSPPST ; 1000: SVILTTMAST ; EGTSGDTGHT ; TAVTDQGSTP ; ATTEISVTPS ; TQKMSTVSTL ; 1050: VTSTQELTSS ; QSQRTGSMGT ; SSKPQATTPT ; EVTTSTLSSF ; SRGSLFSARN ; 1100: CCLQTKKPPL ; PAVVCLPDPS ; SVPSLMHSSK ; PQATTPTEVT ; TSTLSSFSRG ; 1150: STQTQTVSWE ; TSSSGKITAP ; STSSRRTPSV ; ATSDIFTTTD ; STSGNAGHTL ; 1200: LTGSHSVITS ; RVASTTLGRL ; STVAHRQSTQ ; RSSTHSQSYL ; TESMGASSTS ; 1250: ETSLLTEATT ; ETSLCLFTWT ; HCDRDLLSWT ; SSSGLTTKTD ; NDRSTALSAT ; 1300: SLTLPAPSTS ; TASRSTVPPA ; PLPPDQGISL ; FQIGFPLGSL ; CGIPSILQIT ; 1350: VRSFSPSQTT ; MSSPTPTHLK ; EASQEGSVCH ; SGHSGVMLIS ; LAPGEPYFRT ; 1400: TTSHFTMSST ; SLIRKVESLI ; NEFTSDWSFK ; PSDTEVTWVN ; VPAYPAQGRT ; 1450: LGANTYQAIL ; STDGSRSYAL ; FLYQSGGMRW ; DVTQGLYNRV ; LMGFSSGDGY ; 1500: FENSPLIFRP ; AVEKYRPDRF ; LTPNYGSGDS ; RSTGYTGRCG ; PTTGSSVCSG ; 1550: WKVSLSSPAG ; AGTRFPALAP ; GSRDFGSGSS ; TQVCGAGSYA ; ASLRAGRVLY ; 1600: VWHLGEFREG ; WRMHSPWQFD ; EDEGRHRTGL ; AAGTTSPLSA ; SSTSSGGPEL ; 1650: VVLGTRPPRP ; AWTFGDPHIT ; TLDNAKYTFN ; GLGYFLLVQA ; QDRNSSFLLE ; 1700: GRTAQTDSAN ; ATNFIAFAAQ ; YNTSSLKSPI ; TVQWFLEPND ; TIRVVHNNQT ; 1750: VAFNTSDTED ; LPVFNATGVL ; LIQNGSQVSA ; NFDGTVTISV ; IALSNILHAS ; 1800: SSLSEEYRNH ; TKGLLGVWND ; NPEDDFRMPN ; GSTIPSNTSE ; ETLFHYGMTS ; 1850: ETNGIGLLGV ; RTDPLPSEFT ; PIFLSQLWNK ; SGAGEDLISG ; CNEDAQCKFD ; 1900: ILATGNRDIG ; QSTNSILRTF ; RHVNGTLNQY ; PPPIHYSSKI ; QAYKGREQWP ; 1950: LRSPATLRMS ; YSASPTSAVA ; FELFENGSLH ; VDTNIPRRTY ; LEILARDVKT ; 2000: NLSSVLQPET ; VACFCSKEEQ ; CLYNETSKEG ; NSSTEVTSCK ; CDGNSFGRLC ; 2050: EHSKDLCTEP ; CFPNVDCIPG ; KGCQACPPNM ; TGDGRHCVAV ; EISEFCQNHS ; 2100: CPVNYCYNHG ; HCDISGPPDC ; QPTCTCAPAF ; TGNRCFLAGN ; NFTPIIYKEL ; 2150: PLRTITLSLR ; EDENASNADV ; NASVANVLEN ; LDMRAFLSNS ; LVELIRTSPG ; 2200: APVLGKPIHH ; WKVVSHFKYR ; PRGPLIHYLN ; NQLISAVMEA ; FLLQARQERR ; 2250: KRSGEARKNV ; RFFPISRADV ; QDGMALNLSM ; LDEYFTCDGY ; KGYHLVYSPQ ; 2300: DGVTCVSPCS ; EGYCHNGGQC ; KHLPDGPQCT ; CATFSIYTSW ; GERCEHLSVK ; 2344: LGAFFGILFG ; ALGALLLLAI ; LACVVFHFCG ; CSMNKFSYPL ; DSEL
Sequence Length	2344
Sub Unit	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.

Uniprot	Q63661
Gene Name	Muc4
Immunogen Species	Rattus norvegicus (Rat)
Unigene	Rn.24930

Reference	1. "Molecular cloning and sequencing of the mucin subunit of a heterodimeric, bifunctional cell surface glycoprotein complex of ascites rat mammary adenocarcinoma cells." Wu K., Fregien N., Carraway K.L. J. Biol. Chem.269:11950-11955(1994) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] strain: Fischer 344. 2. "Cloning and characterization of the 5' flanking region of the sialomucin complex/rat Muc4 gene: promoter activity in cultured cells." Price-Schiavi S.A., Perez A., Barco R., Carraway K.L. Biochem. J.349:641-649(2000) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-30 3. "Molecular cloning of the transmembrane component of the 13762 mammary adenocarcinoma sialomucin complex. A new member of the epidermal growth factor superfamily." Sheng Z., Wu K., Carraway K.L., Fregien N. J. Biol. Chem.267:16341-16346(1992) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1601-2344;FUNCTION;GLYCOSYLATION strain: Fischer 344. 4. "A complex of two cell surface glycoproteins from ascites mammary adenocarcinoma cells." Sherblom A.P., Carraway K.L. J. Biol. Chem.255:12051-12059(1980) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBUNIT 5. "Post-transcriptional regulation of a milk membrane protein, the sialomucin complex (Ascites sialoglycoprotein (ASGP)-1/ASGP-2, rat muc4), by transforming growth factor beta." Price-Schiavi S.A., Carraway C.A., Fregien N., Carraway K.L. J. Biol. Chem.273:35228-35237(1998) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: POST-TRANSCRIPTIONAL REGULATION 6. "Muc4/sialomucin complex, the intramembrane ErbB2 ligand, induces specific phosphorylation of ErbB2 and enhances expression of p27(kip), but does not activate mitogen-activated kinase or protein kinaseB/Akt pathways." Jepson S., Komatsu M., Haq B., Arango M.E., Huang D., Carraway C.A., Carraway K.L. Oncogene21:7524-7532(2002) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH ERBB2; ERBB3 AND NRG1;PHOSPHORYLATION OF ERBB2 7. "Presence of MUC4 in human milk and at the luminal surfaces of blood vessels." Zhang J., Perez A., Yasin M., Soto P., Rong M., Theodoropoulos G., Carothers Carraway C.A., Carraway K.L. J. Cell. Physiol.204:166-177(2005) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBCELLULAR LOCATION 8. "Muc4-ErbB2 complex formation and signaling in polarized Caco-2 epithelial cells indicate that Muc4 acts as an unorthodox ligand for ErbB2." Ramsauer V.P., Pino V., Farooq A., Carothers Carraway C.A., Salas P.J., Carraway K.L. Mol. Biol. Cell17:2931-2941(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH ERBB2 AND ERBB3

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