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Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a) [Cleaved into: Tumor necrosis factor receptor superfamily member 1A, membrane form; Tumor necrosis factor-binding protein 1 (TBPI)]

 TNR1A_HUMAN             Reviewed;         455 AA.
P19438; A8K4X3; B2RDE4; B3KPQ1; B4DQB7; B4E309; B5M0B5; D3DUR1;
Q9UCA4;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
22-NOV-2017, entry version 221.
RecName: Full=Tumor necrosis factor receptor superfamily member 1A;
AltName: Full=Tumor necrosis factor receptor 1;
Short=TNF-R1;
AltName: Full=Tumor necrosis factor receptor type I;
Short=TNF-RI;
Short=TNFR-I;
AltName: Full=p55;
AltName: Full=p60;
AltName: CD_antigen=CD120a;
Contains:
RecName: Full=Tumor necrosis factor receptor superfamily member 1A, membrane form;
Contains:
RecName: Full=Tumor necrosis factor-binding protein 1;
Short=TBPI;
Flags: Precursor;
Name=TNFRSF1A; Synonyms=TNFAR, TNFR1;
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).
PubMed=2158862; DOI=10.1016/0092-8674(90)90815-V;
Loetscher H., Pan Y.-C.E., Lahm H.-W., Gentz R., Brockhaus M.,
Tabuchi H., Lesslauer W.;
"Molecular cloning and expression of the human 55 kd tumor necrosis
factor receptor.";
Cell 61:351-359(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2158863; DOI=10.1016/0092-8674(90)90816-W;
Schall T.J., Lewis M., Koller K.J., Lee A., Rice G.C., Wong G.H.W.,
Getanaga T., Granger G.A., Lentz R., Raab H., Kohr W.J., Goeddel D.V.;
"Molecular cloning and expression of a receptor for human tumor
necrosis factor.";
Cell 61:361-370(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1702293; DOI=10.1089/dna.1990.9.705;
Himmler A., Maurer-Fogy I., Kroenke M., Scheurich P., Pfizenmaier K.,
Lantz M., Olsson I., Hauptmann R., Stratowa C., Adolf G.R.;
"Molecular cloning and expression of human and rat tumor necrosis
factor receptor chain (p60) and its soluble derivative, tumor necrosis
factor-binding protein.";
DNA Cell Biol. 9:705-715(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 41-53;
110-124 AND 199-201 (ISOFORM 1).
PubMed=1698610;
Nophar Y., Kemper O., Brakebusch C., Engelmann H., Zwang R.,
Aderka D., Holtmann H., Wallach D.;
"Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA
for the type I TNF-R, cloned using amino acid sequence data of its
soluble form, encodes both the cell surface and a soluble form of the
receptor.";
EMBO J. 9:3269-3278(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2170974; DOI=10.1073/pnas.87.19.7380;
Gray P.W., Barrett K., Chantry D., Turner M., Feldman M.;
"Cloning of human tumor necrosis factor (TNF) receptor cDNA and
expression of recombinant soluble TNF-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 87:7380-7384(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1315717; DOI=10.1016/0888-7543(92)90226-I;
Fuchs P., Strehl S., Dworzak M., Himmler A., Ambros P.F.;
"Structure of the human TNF receptor 1 (p60) gene (TNFR1) and
localization to chromosome 12p13.";
Genomics 13:219-224(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-75 AND GLN-121.
SeattleSNPs variation discovery resource;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Neutrophil, Teratocarcinoma, Tongue, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=19906316; DOI=10.1186/1471-2164-10-518;
Wang P., Yu P., Gao P., Shi T., Ma D.;
"Discovery of novel human transcript variants by analysis of intronic
single-block EST with polyadenylation site.";
BMC Genomics 10:518-518(2009).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[11]
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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).
[13]
PROTEIN SEQUENCE OF 41-57 (ISOFORM 1).
TISSUE=Urine;
PubMed=8015639;
Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.;
"Purification of two types of TNF inhibitors in the urine of the
patient with chronic glomerulonephritis.";
Nephron 66:386-390(1994).
[14]
PROTEIN SEQUENCE OF 41-45 (ISOFORM 1).
PubMed=2153136;
Engelmann H., Novick D., Wallach D.;
"Two tumor necrosis factor-binding proteins purified from human urine.
Evidence for immunological cross-reactivity with cell surface tumor
necrosis factor receptors.";
J. Biol. Chem. 265:1531-1536(1990).
[15]
INTERACTION WITH HCV CORE PROTEIN.
PubMed=9557650;
Zhu N., Khoshnan A., Schneider R., Matsumoto M., Dennert G.,
Ware C.F., Lai M.M.C.;
"Hepatitis C virus core protein binds to the cytoplasmic domain of
tumor necrosis factor (TNF) receptor 1 and enhances TNF-induced
apoptosis.";
J. Virol. 72:3691-3697(1998).
[16]
INTERACTION WITH RIPK1 AND SQSTM1.
PubMed=10356400; DOI=10.1093/emboj/18.11.3044;
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB
activation.";
EMBO J. 18:3044-3053(1999).
[17]
INTERACTION WITH FEM1B.
PubMed=10542291; DOI=10.1074/jbc.274.45.32461;
Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y.,
Yu V.C.;
"F1Aalpha, a death receptor-binding protein homologous to the
Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase
substrate that mediates apoptosis.";
J. Biol. Chem. 274:32461-32468(1999).
[18]
INTERACTION WITH GRB2.
PubMed=10359574; DOI=10.1084/jem.189.11.1707;
Hildt E., Oess S.;
"Identification of Grb2 as a novel binding partner of tumor necrosis
factor (TNF) receptor I.";
J. Exp. Med. 189:1707-1714(1999).
[19]
INTERACTION WITH BAG4.
PubMed=9915703; DOI=10.1126/science.283.5401.543;
Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
"Prevention of constitutive TNF receptor 1 signaling by silencer of
death domains.";
Science 283:543-546(1999).
[20]
INTERACTION WITH BABAM2.
PubMed=15465831; DOI=10.1074/jbc.M408678200;
Li Q., Ching A.K.-K., Chan B.C.-L., Chow S.K.-Y., Lim P.-L.,
Ho T.C.-Y., Ip W.-K., Wong C.-K., Lam C.W.-K., Lee K.K.-H.,
Chan J.Y.-H., Chui Y.-L.;
"A death receptor-associated anti-apoptotic protein, BRE, inhibits
mitochondrial apoptotic pathway.";
J. Biol. Chem. 279:52106-52116(2004).
[21]
INTERACTION WITH HHV-5 PROTEIN UL138.
PubMed=21976655; DOI=10.1128/JVI.06005-11;
Le V.T., Trilling M., Hengel H.;
"The cytomegaloviral protein pUL138 acts as potentiator of tumor
necrosis factor (TNF) receptor 1 surface density to enhance ULb'-
encoded modulation of TNF-alpha signaling.";
J. Virol. 85:13260-13270(2011).
[22]
INVOLVEMENT IN MS5, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING
(ISOFORM 4).
PubMed=22801493; DOI=10.1038/nature11307;
Gregory A.P., Dendrou C.A., Attfield K.E., Haghikia A., Xifara D.K.,
Butter F., Poschmann G., Kaur G., Lambert L., Leach O.A., Promel S.,
Punwani D., Felce J.H., Davis S.J., Gold R., Nielsen F.C.,
Siegel R.M., Mann M., Bell J.I., McVean G., Fugger L.;
"TNF receptor 1 genetic risk mirrors outcome of anti-TNF therapy in
multiple sclerosis.";
Nature 488:508-511(2012).
[23]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 30-211 IN COMPLEX WITH TNFB.
PubMed=8387891; DOI=10.1016/0092-8674(93)90132-A;
Banner D.W., D'Arcy A., Janes W., Gentz R., Schoenfeld H.-J.,
Broger C., Loetscher H., Lesslauer W.;
"Crystal structure of the soluble human 55 kd TNF receptor-human TNF
beta complex: implications for TNF receptor activation.";
Cell 73:431-445(1993).
[24]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 41-202.
PubMed=8939750; DOI=10.1016/S0969-2126(96)00134-7;
Naismith J.H., Devine T.Q., Khono H., Sprang S.R.;
"Structures of the extracellular domain of the type I tumor necrosis
factor receptor.";
Structure 4:1251-1262(1996).
[25]
VARIANTS FHF ARG-59; TYR-62; MET-79; PHE-81; ARG-117 AND TYR-117.
PubMed=10199409; DOI=10.1016/S0092-8674(00)80721-7;
McDermott M.F., Aksentijevich I., Galon J., McDermott E.M.,
Ogunkolade B.W., Centola M., Mansfield E., Gadina M., Karenko L.,
Pettersson T., McCarthy J., Frucht D.M., Aringer M., Torosyan Y.,
Teppo A.-M., Wilson M., Karaarslan H.M., Wan Y., Todd I., Wood G.,
Schlimgen R., Kumarajeewa T.R., Cooper S.M., Vella J.P., Amos C.I.,
Mulley J., Quane K.A., Molloy M.G., Rnaki A., Powell R.J.,
Hitman G.A., O'Shea J., Kastner D.L.;
"Germline mutations in the extracellular domains of the 55 kDa TNF
receptor, TNFR1, define a family of dominantly inherited
autoinflammatory syndromes.";
Cell 97:133-144(1999).
[26]
VARIANT FHF SER-59.
PubMed=10902757;
DOI=10.1002/1529-0131(200007)43:7<1535::AID-ANR18>3.0.CO;2-C;
Dode C., Papo T., Fieschi C., Pecheux C., Dion E., Picard F.,
Godeau P., Bienvenu J., Piette J.-C., Delpech M., Grateau G.;
"A novel missense mutation (C30S) in the gene encoding tumor necrosis
factor receptor 1 linked to autosomal-dominant recurrent fever with
localized myositis in a French family.";
Arthritis Rheum. 43:1535-1542(2000).
[27]
VARIANTS FHF GLN-51; SER-59; GLY-62; LEU-75; GLY-115 AND GLN-121.
PubMed=11443543; DOI=10.1086/321976;
Aksentijevich I., Galon J., Soares M., Mansfield E., Hull K.,
Oh H.-H., Goldbach-Mansky R., Dean J., Athreya B., Reginato A.J.,
Henrickson M., Pons-Estel B., O'Shea J.J., Kastner D.L.;
"The tumor-necrosis-factor receptor-associated periodic syndrome: new
mutations in TNFRSF1A, ancestral origins, genotype-phenotype studies,
and evidence for further genetic heterogeneity of periodic fevers.";
Am. J. Hum. Genet. 69:301-314(2001).
[28]
VARIANTS FHF SER-99 AND PRO-121.
PubMed=13130484; DOI=10.1002/art.11215;
Aganna E., Hammond L., Hawkins P.N., Aldea A., McKee S.A.,
Ploos van Amstel H.K., Mischung C., Kusuhara K., Saulsbury F.T.,
Lachmann H.J., Bybee A., McDermott E.M., La Regina M., Arostegui J.I.,
Campistol J.M., Worthington S., High K.P., Molloy M.G., Baker N.,
Bidwell J.L., Castaner J.L., Whiteford M.L., Janssens-Korpola P.L.,
Manna R., Powell R.J., Woo P., Solis P., Minden K., Frenkel J.,
Yague J., Mirakian R.M., Hitman G.A., McDermott M.F.;
"Heterogeneity among patients with tumor necrosis factor receptor-
associated periodic syndrome phenotypes.";
Arthritis Rheum. 48:2632-2644(2003).
[29]
VARIANT FHF SER-99.
PubMed=14610673; DOI=10.1007/s00431-003-1338-0;
Kusuhara K., Nomura A., Nakao F., Hara T.;
"Tumour necrosis factor receptor-associated periodic syndrome with a
novel mutation in the TNFRSF1A gene in a Japanese family.";
Eur. J. Pediatr. 163:30-32(2004).
-!- FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric
TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits
caspase-8 to the activated receptor. The resulting death-inducing
signaling complex (DISC) performs caspase-8 proteolytic activation
which initiates the subsequent cascade of caspases (aspartate-
specific cysteine proteases) mediating apoptosis. Contributes to
the induction of non-cytocidal TNF effects including anti-viral
state and activation of the acid sphingomyelinase.
-!- SUBUNIT: Binding of TNF to the extracellular domain leads to
homotrimerization. The aggregated death domains provide a novel
molecular interface that interacts specifically with the death
domain of TRADD. Various TRADD-interacting proteins such as TRAFS,
RIPK1 and possibly FADD, are recruited to the complex by their
association with TRADD. This complex activates at least two
distinct signaling cascades, apoptosis and NF-kappa-B signaling.
Interacts with BAG4, BABAM2, FEM1B, GRB2, SQSTM1 and TRPC4AP.
Interacts with HCV core protein. Interacts with human
cytomegalovirus/HHV-5 protein UL138. Interacts directly with NOL3
(via CARD domain); inhibits TNF-signaling pathway (By similarity).
{ECO:0000250|UniProtKB:P25118, ECO:0000269|PubMed:10356400,
ECO:0000269|PubMed:10359574, ECO:0000269|PubMed:10542291,
ECO:0000269|PubMed:15465831, ECO:0000269|PubMed:21976655,
ECO:0000269|PubMed:8387891, ECO:0000269|PubMed:9557650,
ECO:0000269|PubMed:9915703}.
-!- INTERACTION:
P28799:GRN; NbExp=4; IntAct=EBI-299451, EBI-747754;
Q969G6:RFK; NbExp=4; IntAct=EBI-299451, EBI-716872;
Q13546:RIPK1; NbExp=6; IntAct=EBI-299451, EBI-358507;
P01375:TNF; NbExp=15; IntAct=EBI-299451, EBI-359977;
Q15628:TRADD; NbExp=13; IntAct=EBI-299451, EBI-359215;
Q12933:TRAF2; NbExp=4; IntAct=EBI-299451, EBI-355744;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22801493};
Single-pass type I membrane protein {ECO:0000269|PubMed:22801493}.
Golgi apparatus membrane {ECO:0000269|PubMed:22801493}; Single-
pass type I membrane protein {ECO:0000269|PubMed:22801493}.
Secreted {ECO:0000269|PubMed:22801493}. Note=A secreted form is
produced through proteolytic processing.
-!- SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Lacks a Golgi-
retention motif, is not membrane bound and therefore is secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=FL-TNFR1;
IsoId=P19438-1; Sequence=Displayed;
Name=2;
IsoId=P19438-2; Sequence=VSP_037153;
Note=No experimental confirmation available.;
Name=4; Synonyms=Delta6-TNFR1;
IsoId=P19438-4; Sequence=VSP_044949;
Note=Disease-associated isoform. Isoform 4 splicing pattern is
driven by a variation in the exon 6/intron 6 boundary region
that alters exon 6 splicing. Exon 6 skipping introduces a
frameshift and the translation of a protein lacking the
intracellular, the transmembrane and part of the extracellular
domain.;
Name=3;
IsoId=P19438-3; Sequence=VSP_037154;
Note=No experimental confirmation available.;
Name=5;
IsoId=P19438-5; Sequence=VSP_047613, VSP_047614;
Note=No experimental confirmation available.;
-!- DOMAIN: The domain that induces A-SMASE is probably identical to
the death domain. The N-SMASE activation domain (NSD) is both
necessary and sufficient for activation of N-SMASE.
-!- DOMAIN: Both the cytoplasmic membrane-proximal region and the C-
terminal region containing the death domain are involved in the
interaction with TRPC4AP. {ECO:0000250}.
-!- PTM: The soluble form is produced from the membrane form by
proteolytic processing.
-!- DISEASE: Familial hibernian fever (FHF) [MIM:142680]: A hereditary
periodic fever syndrome characterized by recurrent fever,
abdominal pain, localized tender skin lesions and myalgia.
Reactive amyloidosis is the main complication and occurs in 25% of
cases. {ECO:0000269|PubMed:10199409, ECO:0000269|PubMed:10902757,
ECO:0000269|PubMed:11443543, ECO:0000269|PubMed:13130484,
ECO:0000269|PubMed:14610673}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Multiple sclerosis 5 (MS5) [MIM:614810]: A
multifactorial, inflammatory, demyelinating disease of the central
nervous system. Sclerotic lesions are characterized by
perivascular infiltration of monocytes and lymphocytes and appear
as indurated areas in pathologic specimens (sclerosis in plaques).
The pathological mechanism is regarded as an autoimmune attack of
the myelin sheath, mediated by both cellular and humoral immunity.
Clinical manifestations include visual loss, extra-ocular movement
disorders, paresthesias, loss of sensation, weakness, dysarthria,
spasticity, ataxia and bladder dysfunction. Genetic and
environmental factors influence susceptibility to the disease.
{ECO:0000269|PubMed:22801493}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. An intronic mutation affecting alternative splicing and
skipping of exon 6 directs increased expression of isoform 4 a
transcript encoding a C-terminally truncated protein which is
secreted and may function as a TNF antagonist.
-!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
autoinflammatory disorders mutations;
URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=2";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tnfrsf1a/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M58286; AAA36753.1; -; mRNA.
EMBL; M33294; AAA03210.1; -; mRNA.
EMBL; M63121; AAA36754.1; -; mRNA.
EMBL; X55313; CAA39021.1; -; mRNA.
EMBL; M60275; AAA36756.1; -; mRNA.
EMBL; M75866; AAA61201.1; -; Genomic_DNA.
EMBL; M75864; AAA61201.1; JOINED; Genomic_DNA.
EMBL; M75865; AAA61201.1; JOINED; Genomic_DNA.
EMBL; AY131997; AAM77802.1; -; Genomic_DNA.
EMBL; AK056611; BAG51763.1; -; mRNA.
EMBL; AK291088; BAF83777.1; -; mRNA.
EMBL; AK298729; BAG60879.1; -; mRNA.
EMBL; AK304517; BAG65321.1; -; mRNA.
EMBL; AK315509; BAG37891.1; -; mRNA.
EMBL; EU927389; ACH57451.1; -; mRNA.
EMBL; AC006057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88805.1; -; Genomic_DNA.
EMBL; CH471116; EAW88806.1; -; Genomic_DNA.
EMBL; BC010140; AAH10140.1; -; mRNA.
CCDS; CCDS8542.1; -. [P19438-1]
PIR; A38208; GQHUT1.
RefSeq; NP_001056.1; NM_001065.3. [P19438-1]
RefSeq; NP_001333020.1; NM_001346091.1. [P19438-2]
RefSeq; NP_001333021.1; NM_001346092.1.
UniGene; Hs.279594; -.
UniGene; Hs.713833; -.
PDB; 1EXT; X-ray; 1.85 A; A/B=41-201.
PDB; 1FT4; X-ray; 2.90 A; A/B=41-201.
PDB; 1ICH; NMR; -; A=345-455.
PDB; 1NCF; X-ray; 2.25 A; A/B=41-201.
PDB; 1TNR; X-ray; 2.85 A; R=44-182.
PDBsum; 1EXT; -.
PDBsum; 1FT4; -.
PDBsum; 1ICH; -.
PDBsum; 1NCF; -.
PDBsum; 1TNR; -.
ProteinModelPortal; P19438; -.
SMR; P19438; -.
BioGrid; 112986; 160.
CORUM; P19438; -.
DIP; DIP-407N; -.
IntAct; P19438; 36.
MINT; MINT-135026; -.
STRING; 9606.ENSP00000162749; -.
BindingDB; P19438; -.
ChEMBL; CHEMBL3378; -.
iPTMnet; P19438; -.
PhosphoSitePlus; P19438; -.
BioMuta; TNFRSF1A; -.
DMDM; 135959; -.
EPD; P19438; -.
MaxQB; P19438; -.
PaxDb; P19438; -.
PeptideAtlas; P19438; -.
PRIDE; P19438; -.
DNASU; 7132; -.
Ensembl; ENST00000162749; ENSP00000162749; ENSG00000067182. [P19438-1]
Ensembl; ENST00000366159; ENSP00000380389; ENSG00000067182. [P19438-5]
GeneID; 7132; -.
KEGG; hsa:7132; -.
UCSC; uc001qnu.4; human. [P19438-1]
CTD; 7132; -.
DisGeNET; 7132; -.
EuPathDB; HostDB:ENSG00000067182.7; -.
GeneCards; TNFRSF1A; -.
HGNC; HGNC:11916; TNFRSF1A.
HPA; CAB010309; -.
HPA; HPA004102; -.
MalaCards; TNFRSF1A; -.
MIM; 142680; phenotype.
MIM; 191190; gene.
MIM; 614810; phenotype.
neXtProt; NX_P19438; -.
OpenTargets; ENSG00000067182; -.
Orphanet; 329967; Intermittent hydrarthrosis.
Orphanet; 802; Multiple sclerosis.
Orphanet; 32960; Tumor necrosis factor receptor 1 associated periodic syndrome.
PharmGKB; PA36609; -.
eggNOG; ENOG410IXBX; Eukaryota.
eggNOG; ENOG4111YG2; LUCA.
GeneTree; ENSGT00530000064001; -.
HOGENOM; HOG000202854; -.
HOVERGEN; HBG058842; -.
InParanoid; P19438; -.
KO; K03158; -.
OMA; GCLEDIE; -.
OrthoDB; EOG091G07LE; -.
PhylomeDB; P19438; -.
TreeFam; TF333916; -.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5626978; TNFR1-mediated ceramide production.
Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-75893; TNF signaling.
SIGNOR; P19438; -.
ChiTaRS; TNFRSF1A; human.
EvolutionaryTrace; P19438; -.
GeneWiki; TNFRSF1A; -.
GenomeRNAi; 7132; -.
PMAP-CutDB; P19438; -.
PRO; PR:P19438; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000067182; -.
CleanEx; HS_TNFRSF1A; -.
ExpressionAtlas; P19438; baseline and differential.
Genevisible; P19438; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043120; F:tumor necrosis factor binding; IBA:GO_Central.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; TAS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:BHF-UCL.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0006693; P:prostaglandin metabolic process; IEA:InterPro.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd08313; Death_TNFR1; 1.
CDD; cd10576; TNFRSF1A; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR020419; TNFR_1A.
InterPro; IPR033994; TNFRSF1A_death.
InterPro; IPR033993; TNFRSF1A_N.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 3.
PRINTS; PR01918; TNFACTORR1A.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 3.
PROSITE; PS50050; TNFR_NGFR_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amyloidosis; Apoptosis;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Golgi apparatus; Host-virus interaction; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 21
CHAIN 22 455 Tumor necrosis factor receptor
superfamily member 1A, membrane form.
/FTId=PRO_0000034543.
CHAIN 41 201 Tumor necrosis factor-binding protein 1.
/FTId=PRO_0000034544.
TOPO_DOM 22 211 Extracellular. {ECO:0000255}.
TRANSMEM 212 234 Helical. {ECO:0000255}.
TOPO_DOM 235 455 Cytoplasmic. {ECO:0000255}.
REPEAT 43 82 TNFR-Cys 1.
REPEAT 83 125 TNFR-Cys 2.
REPEAT 126 166 TNFR-Cys 3.
REPEAT 167 196 TNFR-Cys 4.
DOMAIN 356 441 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 338 348 N-SMase activation domain (NSD).
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 58
DISULFID 59 72
DISULFID 62 81
DISULFID 84 99
DISULFID 102 117
DISULFID 105 125
DISULFID 127 143
DISULFID 146 158
DISULFID 149 166
DISULFID 168 179
DISULFID 182 195
DISULFID 185 191
VAR_SEQ 1 232 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037154.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037153.
VAR_SEQ 184 455 NCKKSLECTKLCLPQIENVKGTEDSGTTVLLPLVIFFGLCL
LSLLFIGLMYRYQRWKSKLYSIVCGKSTPEKEGELEGTTTK
PLAPNPSFSPTPGFTPTLGFSPVPSSTFTSSSTYTPGDCPN
FAAPRREVAPPYQGADPILATALASDPIPNPLQKWEDSAHK
PQSLDTDDPATLYAVVENVPPLRWKEFVRRLGLSDHEIDRL
ELQNGRCLREAQYSMLATWRRRTPRREATLELLGRVLRDMD
LLGCLEDIEEALCGPAALPPAPSLLR -> KHHSAVAPGHF
LWSLPFIPPLHWFNVSLPTVEVQALLHCLWEIDT (in
isoform 4). {ECO:0000305}.
/FTId=VSP_044949.
VAR_SEQ 184 218 NCKKSLECTKLCLPQIENVKGTEDSGTTVLLPLVI -> KV
LLCRPGWNAVARSRLTATSASQIQAILLLQPPK (in
isoform 5).
{ECO:0000303|PubMed:19906316}.
/FTId=VSP_047613.
VAR_SEQ 219 455 Missing (in isoform 5).
{ECO:0000303|PubMed:19906316}.
/FTId=VSP_047614.
VARIANT 51 51 H -> Q (in FHF; dbSNP:rs104895254).
{ECO:0000269|PubMed:11443543}.
/FTId=VAR_019329.
VARIANT 59 59 C -> R (in FHF; dbSNP:rs104895217).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013410.
VARIANT 59 59 C -> S (in FHF; dbSNP:rs104895223).
{ECO:0000269|PubMed:10902757,
ECO:0000269|PubMed:11443543}.
/FTId=VAR_019302.
VARIANT 62 62 C -> G (in FHF; dbSNP:rs104895225).
{ECO:0000269|PubMed:11443543}.
/FTId=VAR_019303.
VARIANT 62 62 C -> Y (in FHF; dbSNP:rs104895218).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013411.
VARIANT 75 75 P -> L (in FHF; may be a polymorphism;
dbSNP:rs4149637).
{ECO:0000269|PubMed:11443543,
ECO:0000269|Ref.7}.
/FTId=VAR_019330.
VARIANT 79 79 T -> M (in FHF; dbSNP:rs104895219).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013412.
VARIANT 81 81 C -> F (in FHF; dbSNP:rs104895220).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013413.
VARIANT 99 99 C -> S (in FHF; dbSNP:rs104895228).
{ECO:0000269|PubMed:13130484,
ECO:0000269|PubMed:14610673}.
/FTId=VAR_019304.
VARIANT 115 115 S -> G (in FHF).
{ECO:0000269|PubMed:11443543}.
/FTId=VAR_019331.
VARIANT 117 117 C -> R (in FHF; dbSNP:rs104895221).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013414.
VARIANT 117 117 C -> Y (in FHF; dbSNP:rs104895222).
{ECO:0000269|PubMed:10199409}.
/FTId=VAR_013415.
VARIANT 121 121 R -> P (in FHF; dbSNP:rs4149584).
{ECO:0000269|PubMed:13130484}.
/FTId=VAR_019305.
VARIANT 121 121 R -> Q (in FHF; unknown pathological
significance; dbSNP:rs4149584).
{ECO:0000269|PubMed:11443543,
ECO:0000269|Ref.7}.
/FTId=VAR_019332.
VARIANT 305 305 P -> T (in dbSNP:rs1804532).
/FTId=VAR_011813.
CONFLICT 13 13 L -> LILPQ (in Ref. 8; BAG51763).
{ECO:0000305}.
CONFLICT 255 255 K -> E (in Ref. 8; BAG37891).
{ECO:0000305}.
CONFLICT 286 286 S -> G (in Ref. 8; BAG51763).
{ECO:0000305}.
CONFLICT 394 394 R -> L (in Ref. 8; BAF83777).
{ECO:0000305}.
CONFLICT 412 412 Missing (in Ref. 5; AAA36756).
{ECO:0000305}.
CONFLICT 443 446 GPAA -> APP (in Ref. 5; AAA36756).
{ECO:0000305}.
STRAND 48 50 {ECO:0000244|PDB:1EXT}.
STRAND 52 54 {ECO:0000244|PDB:1FT4}.
STRAND 58 60 {ECO:0000244|PDB:1EXT}.
STRAND 66 70 {ECO:0000244|PDB:1EXT}.
STRAND 80 83 {ECO:0000244|PDB:1EXT}.
STRAND 92 94 {ECO:0000244|PDB:1EXT}.
HELIX 107 109 {ECO:0000244|PDB:1EXT}.
STRAND 112 115 {ECO:0000244|PDB:1EXT}.
STRAND 124 126 {ECO:0000244|PDB:1EXT}.
STRAND 131 137 {ECO:0000244|PDB:1EXT}.
STRAND 140 145 {ECO:0000244|PDB:1EXT}.
STRAND 152 156 {ECO:0000244|PDB:1EXT}.
STRAND 160 162 {ECO:0000244|PDB:1TNR}.
STRAND 165 168 {ECO:0000244|PDB:1EXT}.
STRAND 172 175 {ECO:0000244|PDB:1EXT}.
STRAND 178 181 {ECO:0000244|PDB:1EXT}.
HELIX 182 184 {ECO:0000244|PDB:1EXT}.
HELIX 192 195 {ECO:0000244|PDB:1EXT}.
HELIX 357 365 {ECO:0000244|PDB:1ICH}.
HELIX 371 378 {ECO:0000244|PDB:1ICH}.
HELIX 382 391 {ECO:0000244|PDB:1ICH}.
HELIX 396 410 {ECO:0000244|PDB:1ICH}.
HELIX 417 427 {ECO:0000244|PDB:1ICH}.
HELIX 431 441 {ECO:0000244|PDB:1ICH}.
SEQUENCE 455 AA; 50495 MW; 4CEFBA96D03B8225 CRC64;
MGLSTVPDLL LPLVLLELLV GIYPSGVIGL VPHLGDREKR DSVCPQGKYI HPQNNSICCT
KCHKGTYLYN DCPGPGQDTD CRECESGSFT ASENHLRHCL SCSKCRKEMG QVEISSCTVD
RDTVCGCRKN QYRHYWSENL FQCFNCSLCL NGTVHLSCQE KQNTVCTCHA GFFLRENECV
SCSNCKKSLE CTKLCLPQIE NVKGTEDSGT TVLLPLVIFF GLCLLSLLFI GLMYRYQRWK
SKLYSIVCGK STPEKEGELE GTTTKPLAPN PSFSPTPGFT PTLGFSPVPS STFTSSSTYT
PGDCPNFAAP RREVAPPYQG ADPILATALA SDPIPNPLQK WEDSAHKPQS LDTDDPATLY
AVVENVPPLR WKEFVRRLGL SDHEIDRLEL QNGRCLREAQ YSMLATWRRR TPRREATLEL
LGRVLRDMDL LGCLEDIEEA LCGPAALPPA PSLLR


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