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ELISA Kit for Rat Tenascin-R

SKU : BHE13810426

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1328r
Alternative Names	Janusin ; Neural recognition molecule J1-160/180 ; Restrictin
Categories	Elisa
Function	Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance.
Specificity	Natural and recombinant Rat Tenascin-R
Subcellular Location	Secreted extracellular space extracellular matrix
Detection Range	1.56-100ng/mL
Entryname	TENR_RAT
Method Type	Sandwich
Platform	PF07974
Protein Name	Tenascin-R
Sensitivity	0.78ng/mL
Sequence	50: MGIEGETVVL ; KNMLIGVNLI ; LLGSMLKPSE ; CRLEVTTERV ; QRQTVEEEGG ; 100: ASSYNTSSKE ; QPMVFNHVYN ; INVPLESLCS ; SGLEASAEQD ; VSAEDDTLAE ; 150: YTGQTSDHES ; QVTFTHKINL ; PKKACPCASS ; AQVLQELLSR ; IEMLEREVSV ; 200: LRDQCNTNCC ; QESAATGQLD ; YVPHCSGHGN ; FSFESCGCIC ; NEGWFGKNCS ; 250: EPYCPLGCSS ; RGVCVDGQCI ; CDSEYSGDDC ; SELRCPTDCS ; SRGLCVDGEC ; 300: VCEEPYTGED ; CRELRCPGDC ; SGKGQCANGT ; CLCQEGYAGE ; DCSQRRCLNA ; 350: CSGRGHCQEG ; LCICEEGYQG ; PDCSAVTPPE ; DLRVAGISDR ; SIELEWDGPM ; 400: AVTEYVISYQ ; PSLGGLQLQQ ; RVPGDWSGVT ; ITELEPGLTY ; NISVYAVISN ; 450: ILSLPITAKV ; ATHLSTPQGL ; QFKTITETTV ; EVQWEPFSFS ; FDGWEISFTP ; 500: KNNEGGVIAQ ; LPSDVTSFNQ ; TGLKPGEEYI ; VNVVALKEQA ; RGPPTSASVS ; 550: TVIDGPTQIL ; VRDVSDTVAF ; VEWTPPRAKV ; DFILLKYGLV ; GGEGGKTTFR ; 600: LQPPLSQYSV ; QALRPGSRYE ; VSISAVRGTN ; ESDASSTQFT ; TEIDAPKNLR ; 650: VGSRTATSLD ; LEWDNSEAEA ; QEYKVVYSTL ; AGEQYHEVLV ; PKGIGPTTKT ; 700: TLTDLVPGTE ; YGVGISAVMN ; SKQSIPATMN ; ARTELDSPRD ; LMVTASSETS ; 750: ISLIWTKASG ; PIDHYRITFT ; PSSGISSEVT ; VPRDRTSYTL ; TDLEPGAEYI ; 800: ISITAERGRQ ; QSLESTVDAF ; TGFRPISHLH ; FSHVTSSSVN ; ITWSDPSPPA ; 850: DRLILNYSPR ; DEEEEMMEVL ; LDATKRHAVL ; MGLQPATEYI ; VNLVAVHGTV ; 900: TSEPIVGSIT ; TGIDPPKNIT ; ISNVTKDSLT ; VSWSPPVAPF ; DYYEYPIDHP ; 950: SGRLDSSVVP ; NTVTEFTITR ; LYPASQYEIS ; LNSVRGREES ; ERICTLVHTA ; 1000: MDSPMDLIAT ; NITPTEALLQ ; WKAPMGEVEN ; YVIVLTHFAM ; AGETILVDGV ; 1050: SEEFQLVDLL ; PRTHYTVTMY ; ATSGPLVSGT ; IATNFSTLLD ; PPANLTASEV ; 1100: TRQSALISWQ ; PPRAAIENYV ; LTYKSTDGSR ; KELIVDAEDT ; WIRLEGLSEN ; 1150: TDYTVLLQAA ; QEATRSSLTS ; TIFTTGGRVF ; SHPQDCAQHL ; MNGDTLSGVY ; 1200: TIFLNGELSH ; KLQVYCDMTT ; DGGGWIVFQR ; RQNGQTDFFR ; KWADYRVGFG ; 1250: NLEDEFWLGL ; DNYHRITAQG ; RYELRVDMRD ; GQEAVFAYYD ; KFAVEDSRSL ; 1300: YKLRIGGYNG ; TAGDSLSYHQ ; GRPFSTEDRD ; NDVAVTNCAM ; SYKGAWWYKN ; 1350: CHRTNLNGKY ; GESRHSQGIN ; WYHWKGHEFS ; IPFVEMKMRP ; YIHRLTAGRK ; 1356: RRALKF
Sequence Length	1356
String	Q05546
Sub Unit	Forms oligomers. Interacts with TNC and FN1 (By similarity). Interacts with BCAN and AGC1 in a calcium -dependent manner. Interacts with CNTN1, SCN2B, PTPRZ1, and CSPG3.

Uniprot	Q05546
Gene Name	Tnr
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:25567
Unigene	Rn.11028

Reference	1. "Molecular characterization and in situ mRNA localization of the neural recognition molecule J1-160/180: a modular structure similar to tenascin." Fuss B., Wintergerst E.-S., Bartsch U., Schachner M. J. Cell Biol.120:1237-1249(1993) [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] (ISOFORMS 1 AND 2);DEVELOPMENTAL STAGE;TISSUE SPECIFICITY 2. "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11." Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M. Eur. J. Neurosci.8:766-782(1996) [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 CNTN1 3. "The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety." Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D., Schachner M., Ruoslahti E., Yamaguchi Y. Proc. Natl. Acad. Sci. U.S.A.94:10116-10121(1997) [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 BCAN 4. "Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R." Srinivasan J., Schachner M., Catterall W.A. Proc. Natl. Acad. Sci. U.S.A.95:15753-15757(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: INTERACTION WITH SCN2B;FUNCTION 5. "High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule." Milev P., Chiba A., Haring M., Rauvala H., Schachner M., Ranscht B., Margolis R.K., Margolis R.U. J. Biol. Chem.273:6998-7005(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: INTERACTION WITH PTPRZ1 AND CSPG3 6. "Chondroitin sulfates expressed on oligodendrocyte-derived tenascin-R are involved in neural cell recognition. Functional implications during CNS development and regeneration." Probstmeier R., Stichel C.C., Muller H.W., Asou H., Pesheva P. J. Neurosci. Res.60:21-36(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: GLYCOSYLATION;FUNCTION 7. "Spatial and temporal regulation of tenascin-R glycosylation in the cerebellum." Woodworth A., Fiete D., Baenziger J.U. J. Biol. Chem.277:50941-50947(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: GLYCOSYLATION 8. "Neuronal-specific synthesis and glycosylation of tenascin-R." Woodworth A., Pesheva P., Fiete D., Baenziger J.U. J. Biol. Chem.279:10413-10421(2004) [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: GLYCOSYLATION;DEVELOPMENTAL STAGE;FUNCTION 9. "Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins." Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A., Logan D.T. Structure12:1495-1506(2004) [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: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 489-771;INTERACTION WITH ACAN

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