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Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]

 TNFA_HUMAN              Reviewed;         233 AA.
P01375; O43647; Q9P1Q2; Q9UIV3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 228.
RecName: Full=Tumor necrosis factor;
AltName: Full=Cachectin;
AltName: Full=TNF-alpha;
AltName: Full=Tumor necrosis factor ligand superfamily member 2;
Short=TNF-a;
Contains:
RecName: Full=Tumor necrosis factor, membrane form;
AltName: Full=N-terminal fragment;
Short=NTF;
Contains:
RecName: Full=Intracellular domain 1;
Short=ICD1;
Contains:
RecName: Full=Intracellular domain 2;
Short=ICD2;
Contains:
RecName: Full=C-domain 1;
Contains:
RecName: Full=C-domain 2;
Contains:
RecName: Full=Tumor necrosis factor, soluble form;
Flags: Precursor;
Name=TNF; Synonyms=TNFA, TNFSF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3555974;
Nedospasov S.A., Shakhov A.N., Turetskaya R.L., Mett V.A.,
Azizov M.M., Georgiev G.P., Korobko V.G., Dobrynin V.N.,
Filippov S.A., Bystrov N.S., Boldyreva E.F., Chuvpilo S.A.,
Chumakov A.M., Shingarova L.N., Ovchinnikov Y.A.;
"Tandem arrangement of genes coding for tumor necrosis factor (TNF-
alpha) and lymphotoxin (TNF-beta) in the human genome.";
Cold Spring Harb. Symp. Quant. Biol. 51:611-624(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6392892; DOI=10.1038/312724a0;
Pennica D., Nedwin G.E., Hayflick J.S., Seeburg P.H., Derynck R.,
Palladino M.A., Kohr W.J., Aggarwal B.B., Goeddel D.V.;
"Human tumour necrosis factor: precursor structure, expression and
homology to lymphotoxin.";
Nature 312:724-729(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=3883195; DOI=10.1038/313803a0;
Shirai T., Yamaguchi H., Ito H., Todd C.W., Wallace R.B.;
"Cloning and expression in Escherichia coli of the gene for human
tumour necrosis factor.";
Nature 313:803-806(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2995927; DOI=10.1093/nar/13.17.6361;
Nedwin G.E., Naylor S.L., Sakaguchi A.Y., Smith D.H.,
Jarrett-Nedwin J., Pennica D., Goeddel D.V., Gray P.W.;
"Human lymphotoxin and tumor necrosis factor genes: structure,
homology and chromosomal localization.";
Nucleic Acids Res. 13:6361-6373(1985).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3856324; DOI=10.1126/science.3856324;
Wang A.M., Creasey A.A., Ladner M.B., Lin L.S., Strickler J.,
van Arsdell J.N., Yamamoto R., Mark D.F.;
"Molecular cloning of the complementary DNA for human tumor necrosis
factor.";
Science 228:149-154(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3932069; DOI=10.1111/j.1432-1033.1985.tb09226.x;
Marmenout A., Fransen L., Tavernier J., van der Heyden J., Tizard R.,
Kawashima E., Shaw A., Johnson M.J., Semon D., Mueller R.,
Ruysschaert M.-R., van Vliet A., Fiers W.;
"Molecular cloning and expression of human tumor necrosis factor and
comparison with mouse tumor necrosis factor.";
Eur. J. Biochem. 152:515-522(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8499947; DOI=10.1038/ng0293-137;
Iris F.J.M., Bougueleret L., Prieur S., Caterina D., Primas G.,
Perrot V., Jurka J., Rodriguez-Tome P., Claverie J.-M., Dausset J.,
Cohen D.;
"Dense Alu clustering and a potential new member of the NF kappa B
family within a 90 kilobase HLA class III segment.";
Nat. Genet. 3:137-145(1993).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10202016;
Neville M.J., Campbell R.D.;
"A new member of the Ig superfamily and a V-ATPase G subunit are among
the predicted products of novel genes close to the TNF locus in the
human MHC.";
J. Immunol. 162:4745-4754(1999).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
"Genome diversity in HLA: a new strategy for detection of genetic
polymorphisms in expressed genes within the HLA class III and class I
regions.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-84.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
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).
[15]
PROTEIN SEQUENCE OF 77-99, AND GLYCOSYLATION AT SER-80.
PubMed=8631363; DOI=10.1111/j.1432-1033.1996.00431.x;
Takakura-Yamamoto R., Yamamoto S., Fukuda S., Kurimoto M.;
"O-glycosylated species of natural human tumor-necrosis factor-
alpha.";
Eur. J. Biochem. 235:431-437(1996).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-233.
Jang J.S., Kim B.E.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 84-214.
TISSUE=Prostatic carcinoma;
Shao C., Yan W., Zhu F., Yue W., Chai Y., Zhao Z., Wang C.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[18]
PHOSPHORYLATION (MEMBRANE FORM).
PubMed=8597870;
Pocsik E., Duda E., Wallach D.;
"Phosphorylation of the 26 kDa TNF precursor in monocytic cells and in
transfected HeLa cells.";
J. Inflamm. 45:152-160(1995).
[19]
PHOSPHORYLATION BY CK1, AND DEPHOSPHORYLATION.
PubMed=10205166; DOI=10.1093/emboj/18.8.2119;
Watts A.D., Hunt N.H., Wanigasekara Y., Bloomfield G., Wallach D.,
Roufogalis B.D., Chaudhri G.;
"A casein kinase I motif present in the cytoplasmic domain of members
of the tumour necrosis factor ligand family is implicated in 'reverse
signalling'.";
EMBO J. 18:2119-2126(1999).
[20]
MUTAGENESIS.
PubMed=2009860;
Ostade X.V., Tavernier J., Prange T., Fiers W.;
"Localization of the active site of human tumour necrosis factor
(hTNF) by mutational analysis.";
EMBO J. 10:827-836(1991).
[21]
MYRISTOYLATION AT LYS-19 AND LYS-20.
PubMed=1402651; DOI=10.1084/jem.176.4.1053;
Stevenson F.T., Bursten S.L., Locksley R.M., Lovett D.H.;
"Myristyl acylation of the tumor necrosis factor alpha precursor on
specific lysine residues.";
J. Exp. Med. 176:1053-1062(1992).
[22]
CLEAVAGE BY ADAM17.
PubMed=9034191; DOI=10.1038/385733a0;
Moss M.L., Jin S.-L.C., Milla M.E., Burkhart W., Carter H.L.,
Chen W.-J., Clay W.C., Didsbury J.R., Hassler D., Hoffman C.R.,
Kost T.A., Lambert M.H., Leesnitzer M.A., McCauley P., McGeehan G.,
Mitchell J., Moyer M., Pahel G., Rocque W., Overton L.K., Schoenen F.,
Seaton T., Su J.-L., Warner J., Willard D., Becherer J.D.;
"Cloning of a disintegrin metalloproteinase that processes precursor
tumour-necrosis factor-alpha.";
Nature 385:733-736(1997).
[23]
POLYMORPHISM, AND INVOLVEMENT IN SUSCEPTIBILITY TO MALARIA.
PubMed=10369255; DOI=10.1038/9649;
Knight J.C., Udalova I., Hill A.V., Greenwood B.M., Peshu N.,
Marsh K., Kwiatkowski D.;
"A polymorphism that affects OCT-1 binding to the TNF promoter region
is associated with severe malaria.";
Nat. Genet. 22:145-150(1999).
[24]
FUNCTION OF TNF INTRACELLULAR DOMAIN, CLEAVAGE BY SPPL2A AND SPPL2B,
AND SUBCELLULAR LOCATION.
PubMed=16829952; DOI=10.1038/ncb1440;
Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S.,
Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B.;
"SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in
activated dendritic cells to trigger IL-12 production.";
Nat. Cell Biol. 8:843-848(2006).
[25]
CLEAVAGE BY SPPL2A AND SPPL2B, CLEAVAGE SITE, INTERACTION WITH SPPL2B,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16829951; DOI=10.1038/ncb1450;
Fluhrer R., Grammer G., Israel L., Condron M.M., Haffner C.,
Friedmann E., Bohland C., Imhof A., Martoglio B., Teplow D.B.,
Haass C.;
"A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD
aspartyl protease SPPL2b.";
Nat. Cell Biol. 8:894-896(2006).
[26]
FUNCTION.
PubMed=22517918; DOI=10.1189/jlb.1211623;
Jinesh G.G., Chunduru S., Kamat A.M.;
"Smac mimetic enables the anticancer action of BCG-stimulated
neutrophils through TNF-alpha but not through TRAIL and FasL.";
J. Leukoc. Biol. 92:233-244(2012).
[27]
FUNCTION.
PubMed=23396208; DOI=10.1038/nm.3085;
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
Chen X., Wan B., Chin Y.E., Zhang J.Z.;
"Phosphorylation of FOXP3 controls regulatory T cell function and is
inhibited by TNF-alpha in rheumatoid arthritis.";
Nat. Med. 19:322-328(2013).
[28]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=2922050; DOI=10.1038/338225a0;
Jones E.Y., Stuart D.I., Walker N.P.;
"Structure of tumour necrosis factor.";
Nature 338:225-228(1989).
[29]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=1964681;
Jones E.Y., Stuart D.I., Walker N.P.;
"The structure of tumour necrosis factor -- implications for
biological function.";
J. Cell Sci. Suppl. 13:11-18(1990).
[30]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=2551905;
Eck M.J., Sprang S.R.;
"The structure of tumor necrosis factor-alpha at 2.6-A resolution.
Implications for receptor binding.";
J. Biol. Chem. 264:17595-17605(1989).
[31]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ARG-107.
PubMed=9488135; DOI=10.1093/protein/10.10.1101;
Reed C., Fu Z.Q., Wu J., Xue Y.N., Harrison R.W., Chen M.J.,
Weber I.T.;
"Crystal structure of TNF-alpha mutant R31D with greater affinity for
receptor R1 compared with R2.";
Protein Eng. 10:1101-1107(1997).
[32]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT SER-3.
PubMed=9442056; DOI=10.1074/jbc.273.4.2153;
Cha S.S., Kim J.S., Cho H.S., Shin N.K., Jeong W., Shin H.C.,
Kim Y.J., Hahn J.H., Oh B.H.;
"High resolution crystal structure of a human tumor necrosis factor-
alpha mutant with low systemic toxicity.";
J. Biol. Chem. 273:2153-2160(1998).
[33]
INVOLVEMENT IN PSORIATIC ARTHRITIS SUSCEPTIBILITY.
PubMed=12746914; DOI=10.1002/art.10935;
Balding J., Kane D., Livingstone W., Mynett-Johnson L., Bresnihan B.,
Smith O., FitzGerald O.;
"Cytokine gene polymorphisms: association with psoriatic arthritis
susceptibility and severity.";
Arthritis Rheum. 48:1408-1413(2003).
[34]
INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION.
PubMed=12915457; DOI=10.1093/hmg/ddg262;
Kim Y.J., Lee H.-S., Yoon J.-H., Kim C.Y., Park M.H., Kim L.H.,
Park B.L., Shin H.D.;
"Association of TNF-alpha promoter polymorphisms with the clearance of
hepatitis B virus infection.";
Hum. Mol. Genet. 12:2541-2546(2003).
-!- FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and
TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can
induce cell death of certain tumor cell lines. It is potent
pyrogen causing fever by direct action or by stimulation of
interleukin-1 secretion and is implicated in the induction of
cachexia, Under certain conditions it can stimulate cell
proliferation and induce cell differentiation. Impairs regulatory
T-cells (Treg) function in individuals with rheumatoid arthritis
via FOXP3 dephosphorylation. Upregulates the expression of protein
phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418'
residue of FOXP3, thereby inactivating FOXP3 and rendering Treg
cells functionally defective (PubMed:23396208). Key mediator of
cell death in the anticancer action of BCG-stimulated neutrophils
in combination with DIABLO/SMAC mimetic in the RT4v6 bladder
cancer cell line (PubMed:22517918). {ECO:0000269|PubMed:16829952,
ECO:0000269|PubMed:22517918, ECO:0000269|PubMed:23396208}.
-!- FUNCTION: The TNF intracellular domain (ICD) form induces IL12
production in dendritic cells. {ECO:0000269|PubMed:16829952}.
-!- SUBUNIT: Homotrimer. Interacts with SPPL2B.
{ECO:0000269|PubMed:16829951}.
-!- INTERACTION:
Q8UYL3:crmE (xeno); NbExp=3; IntAct=EBI-359977, EBI-7539950;
Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-359977, EBI-81279;
P19438:TNFRSF1A; NbExp=12; IntAct=EBI-359977, EBI-299451;
P20333:TNFRSF1B; NbExp=2; IntAct=EBI-359977, EBI-358983;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16829952};
Single-pass type II membrane protein
{ECO:0000269|PubMed:16829952}.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor, membrane form:
Membrane; Single-pass type II membrane protein.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor, soluble form:
Secreted.
-!- SUBCELLULAR LOCATION: C-domain 1: Secreted.
-!- SUBCELLULAR LOCATION: C-domain 2: Secreted.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing. The membrane-bound form is further
proteolytically processed by SPPL2A or SPPL2B through regulated
intramembrane proteolysis producing TNF intracellular domains
(ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-
domain 2 secreted into the extracellular space.
{ECO:0000269|PubMed:16829951, ECO:0000269|PubMed:16829952,
ECO:0000269|PubMed:9034191}.
-!- PTM: The membrane form, but not the soluble form, is
phosphorylated on serine residues. Dephosphorylation of the
membrane form occurs by binding to soluble TNFRSF1A/TNFR1.
{ECO:0000269|PubMed:10205166, ECO:0000269|PubMed:8597870}.
-!- PTM: O-glycosylated; glycans contain galactose, N-
acetylgalactosamine and N-acetylneuraminic acid.
{ECO:0000269|PubMed:8631363}.
-!- POLYMORPHISM: Genetic variations in TNF influence susceptibility
to hepatitis B virus (HBV) infection [MIM:610424].
-!- POLYMORPHISM: Genetic variations in TNF are involved in
susceptibility to malaria [MIM:611162].
-!- DISEASE: Psoriatic arthritis (PSORAS) [MIM:607507]: An
inflammatory, seronegative arthritis associated with psoriasis. It
is a heterogeneous disorder ranging from a mild, non-destructive
disease to a severe, progressive, erosive arthropathy. Five types
of psoriatic arthritis have been defined: asymmetrical
oligoarthritis characterized by primary involvement of the small
joints of the fingers or toes; asymmetrical arthritis which
involves the joints of the extremities; symmetrical polyarthritis
characterized by a rheumatoid like pattern that can involve hands,
wrists, ankles, and feet; arthritis mutilans, which is a rare but
deforming and destructive condition; arthritis of the sacroiliac
joints and spine (psoriatic spondylitis).
{ECO:0000269|PubMed:12746914}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF71992.1; Type=Frameshift; Positions=91, 157; Evidence={ECO:0000305};
Sequence=CAA75070.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Tumor necrosis factor alpha
entry;
URL="https://en.wikipedia.org/wiki/Tumor_necrosis_factor-alpha";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TNFaID319.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tnf/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tnf/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=TNF";
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EMBL; M16441; AAA61200.1; -; Genomic_DNA.
EMBL; X02910; CAA26669.1; -; Genomic_DNA.
EMBL; X01394; CAA25650.1; -; mRNA.
EMBL; M10988; AAA61198.1; -; mRNA.
EMBL; M26331; AAA36758.1; -; Genomic_DNA.
EMBL; Z15026; CAA78745.1; -; Genomic_DNA.
EMBL; Y14768; CAA75070.1; ALT_SEQ; Genomic_DNA.
EMBL; AF129756; AAD18091.1; -; Genomic_DNA.
EMBL; BA000025; BAB63396.1; -; Genomic_DNA.
EMBL; AB088112; BAC54944.1; -; Genomic_DNA.
EMBL; AY066019; AAL47581.1; -; Genomic_DNA.
EMBL; AY214167; AAO21132.1; -; Genomic_DNA.
EMBL; BC028148; AAH28148.1; -; mRNA.
EMBL; AF043342; AAC03542.1; -; mRNA.
EMBL; AF098751; AAF71992.1; ALT_FRAME; mRNA.
CCDS; CCDS4702.1; -.
PIR; A93585; QWHUN.
RefSeq; NP_000585.2; NM_000594.3.
UniGene; Hs.241570; -.
PDB; 1A8M; X-ray; 2.30 A; A/B/C=77-233.
PDB; 1TNF; X-ray; 2.60 A; A/B/C=77-233.
PDB; 2AZ5; X-ray; 2.10 A; A/B/C/D=86-233.
PDB; 2E7A; X-ray; 1.80 A; A/B/C=77-233.
PDB; 2TUN; X-ray; 3.10 A; A/B/C/D/E/F=77-233.
PDB; 2ZJC; X-ray; 2.50 A; A/B/C=77-233.
PDB; 2ZPX; X-ray; 2.83 A; A/B/C=77-233.
PDB; 3ALQ; X-ray; 3.00 A; A/B/C/D/E/F=77-233.
PDB; 3IT8; X-ray; 2.80 A; A/B/C/G/H/I=82-233.
PDB; 3L9J; X-ray; 2.10 A; T=85-233.
PDB; 3WD5; X-ray; 3.10 A; A=77-233.
PDB; 4G3Y; X-ray; 2.60 A; C=77-233.
PDB; 4TSV; X-ray; 1.80 A; A=84-233.
PDB; 4TWT; X-ray; 2.85 A; A/B/C/D=77-233.
PDB; 4Y6O; X-ray; 1.60 A; C/D=17-23.
PDB; 5MU8; X-ray; 3.00 A; A/B/C/D/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e=77-233.
PDB; 5TSW; X-ray; 2.50 A; A/B/C/D/E/F=84-233.
PDBsum; 1A8M; -.
PDBsum; 1TNF; -.
PDBsum; 2AZ5; -.
PDBsum; 2E7A; -.
PDBsum; 2TUN; -.
PDBsum; 2ZJC; -.
PDBsum; 2ZPX; -.
PDBsum; 3ALQ; -.
PDBsum; 3IT8; -.
PDBsum; 3L9J; -.
PDBsum; 3WD5; -.
PDBsum; 4G3Y; -.
PDBsum; 4TSV; -.
PDBsum; 4TWT; -.
PDBsum; 4Y6O; -.
PDBsum; 5MU8; -.
PDBsum; 5TSW; -.
ProteinModelPortal; P01375; -.
SMR; P01375; -.
BioGrid; 112979; 100.
CORUM; P01375; -.
DIP; DIP-2895N; -.
IntAct; P01375; 39.
MINT; MINT-1131842; -.
STRING; 9606.ENSP00000398698; -.
BindingDB; P01375; -.
ChEMBL; CHEMBL1825; -.
DrugBank; DB05250; 681323.
DrugBank; DB00051; Adalimumab.
DrugBank; DB04956; Afelimomab.
DrugBank; DB05879; AME-527.
DrugBank; DB01427; Amrinone.
DrugBank; DB05676; Apremilast.
DrugBank; DB05066; AV411.
DrugBank; DB08904; Certolizumab pegol.
DrugBank; DB00608; Chloroquine.
DrugBank; DB01407; Clenbuterol.
DrugBank; DB05744; CRx-139.
DrugBank; DB05869; CTI-01.
DrugBank; DB05758; CYT007-TNFQb.
DrugBank; DB00668; Epinephrine.
DrugBank; DB00005; Etanercept.
DrugBank; DB01296; Glucosamine.
DrugBank; DB06674; Golimumab.
DrugBank; DB05767; HMPL-004.
DrugBank; DB00065; Infliximab.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB05303; OMS-103HP.
DrugBank; DB05218; PN0621.
DrugBank; DB08910; Pomalidomide.
DrugBank; DB01411; Pranlukast.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB05412; SCIO-469.
DrugBank; DB05207; SD118.
DrugBank; DB01041; Thalidomide.
DrugBank; DB05470; VX-702.
DrugBank; DB05017; YSIL6.
iPTMnet; P01375; -.
PhosphoSitePlus; P01375; -.
SwissPalm; P01375; -.
UniCarbKB; P01375; -.
BioMuta; TNF; -.
DMDM; 135934; -.
PaxDb; P01375; -.
PeptideAtlas; P01375; -.
PRIDE; P01375; -.
DNASU; 7124; -.
Ensembl; ENST00000376122; ENSP00000365290; ENSG00000204490.
Ensembl; ENST00000383496; ENSP00000372988; ENSG00000206439.
Ensembl; ENST00000412275; ENSP00000392858; ENSG00000228321.
Ensembl; ENST00000420425; ENSP00000410668; ENSG00000228849.
Ensembl; ENST00000443707; ENSP00000389492; ENSG00000230108.
Ensembl; ENST00000448781; ENSP00000389490; ENSG00000223952.
Ensembl; ENST00000449264; ENSP00000398698; ENSG00000232810.
GeneID; 7124; -.
KEGG; hsa:7124; -.
CTD; 7124; -.
DisGeNET; 7124; -.
EuPathDB; HostDB:ENSG00000232810.3; -.
GeneCards; TNF; -.
H-InvDB; HIX0165948; -.
HGNC; HGNC:11892; TNF.
MalaCards; TNF; -.
MIM; 191160; gene.
MIM; 607507; phenotype.
MIM; 610424; phenotype.
MIM; 611162; phenotype.
neXtProt; NX_P01375; -.
OpenTargets; ENSG00000232810; -.
Orphanet; 40050; Adult psoriatic arthritis.
PharmGKB; PA435; -.
eggNOG; ENOG410ISAN; Eukaryota.
eggNOG; ENOG410YQC4; LUCA.
GeneTree; ENSGT00530000062992; -.
HOGENOM; HOG000048729; -.
HOVERGEN; HBG012516; -.
InParanoid; P01375; -.
KO; K03156; -.
OMA; PWYEPIY; -.
OrthoDB; EOG091G0HIG; -.
PhylomeDB; P01375; -.
TreeFam; TF332169; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
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-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-75893; TNF signaling.
SIGNOR; P01375; -.
ChiTaRS; TNF; human.
EvolutionaryTrace; P01375; -.
GeneWiki; Tumor_necrosis_factor-alpha; -.
GenomeRNAi; 7124; -.
PMAP-CutDB; P01375; -.
PRO; PR:P01375; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000232810; -.
CleanEx; HS_TNF; -.
ExpressionAtlas; P01375; baseline and differential.
Genevisible; P01375; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0001891; C:phagocytic cup; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055037; C:recycling endosome; ISS:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:BHF-UCL.
GO; GO:0000185; P:activation of MAPKKK activity; IDA:BHF-UCL.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; IDA:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IMP:BHF-UCL.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0071550; P:death-inducing signaling complex assembly; TAS:Reactome.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0048566; P:embryonic digestive tract development; IEP:DFLAT.
GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
GO; GO:0050901; P:leukocyte tethering or rolling; IDA:BHF-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0097527; P:necroptotic signaling pathway; IDA:UniProtKB.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IEA:Ensembl.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IDA:UniProtKB.
GO; GO:0061048; P:negative regulation of branching involved in lung morphogenesis; IDA:UniProtKB.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; NAS:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0046325; P:negative regulation of glucose import; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
GO; GO:0010888; P:negative regulation of lipid storage; NAS:BHF-UCL.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IDA:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0043242; P:negative regulation of protein complex disassembly; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2000334; P:positive regulation of blood microparticle formation; IDA:BHF-UCL.
GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; TAS:Reactome.
GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IDA:BHF-UCL.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IDA:BHF-UCL.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0002876; P:positive regulation of chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; IDA:BHF-UCL.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; NAS:BHF-UCL.
GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
GO; GO:1904999; P:positive regulation of leukocyte adhesion to arterial endothelial cell; IDA:BHF-UCL.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IDA:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; NAS:BHF-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IDA:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; IDA:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
GO; GO:0071803; P:positive regulation of podosome assembly; IDA:BHF-UCL.
GO; GO:0043068; P:positive regulation of programmed cell death; IDA:UniProtKB.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0043243; P:positive regulation of protein complex disassembly; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0051222; P:positive regulation of protein transport; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0060557; P:positive regulation of vitamin D biosynthetic process; IDA:BHF-UCL.
GO; GO:0000060; P:protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0032800; P:receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; IDA:BHF-UCL.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
GO; GO:0009651; P:response to salt stress; TAS:BHF-UCL.
GO; GO:0009615; P:response to virus; IDA:BHF-UCL.
GO; GO:0030730; P:sequestering of triglyceride; IDA:BHF-UCL.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:BHF-UCL.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR006053; TNF.
InterPro; IPR002959; TNF_alpha.
InterPro; IPR021184; TNF_CS.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
PANTHER; PTHR11471:SF46; PTHR11471:SF46; 1.
Pfam; PF00229; TNF; 1.
PRINTS; PR01234; TNECROSISFCT.
PRINTS; PR01235; TNFALPHA.
SMART; SM00207; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS00251; TNF_1; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein; Lipoprotein;
Membrane; Myristate; Phosphoprotein; Polymorphism; Reference proteome;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 233 Tumor necrosis factor, membrane form.
/FTId=PRO_0000034423.
CHAIN 1 39 Intracellular domain 1.
/FTId=PRO_0000417231.
CHAIN 1 35 Intracellular domain 2.
/FTId=PRO_0000417232.
CHAIN 50 ? C-domain 1.
/FTId=PRO_0000417233.
CHAIN 52 ? C-domain 2.
/FTId=PRO_0000417234.
CHAIN 77 233 Tumor necrosis factor, soluble form.
{ECO:0000269|PubMed:3856324}.
/FTId=PRO_0000034424.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 233 Extracellular. {ECO:0000255}.
SITE 35 36 Cleavage; by SPPL2A or SPPL2B.
SITE 39 40 Cleavage; by SPPL2A or SPPL2B.
SITE 49 50 Cleavage; by SPPL2A or SPPL2B.
SITE 51 52 Cleavage; by SPPL2A or SPPL2B.
SITE 76 77 Cleavage; by ADAM17.
MOD_RES 2 2 Phosphoserine; by CK1. {ECO:0000305}.
LIPID 19 19 N6-myristoyl lysine.
{ECO:0000269|PubMed:1402651}.
LIPID 20 20 N6-myristoyl lysine.
{ECO:0000269|PubMed:1402651}.
CARBOHYD 80 80 O-linked (GalNAc...) serine; in soluble
form. {ECO:0000269|PubMed:8631363}.
DISULFID 145 177
VARIANT 84 84 P -> L (in dbSNP:rs4645843).
{ECO:0000269|Ref.13}.
/FTId=VAR_019378.
VARIANT 94 94 A -> T (in dbSNP:rs1800620).
/FTId=VAR_011927.
MUTAGEN 105 105 L->S: Low activity.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 108 108 R->W: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 112 112 L->F: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 160 160 A->V: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 162 162 S->F: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 167 167 V->A,D: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
MUTAGEN 222 222 E->K: Biologically inactive.
{ECO:0000269|PubMed:2009860}.
CONFLICT 63 63 F -> S (in Ref. 5; AAA61198).
{ECO:0000305}.
CONFLICT 84 86 PSD -> VNR (in Ref. 17; AAF71992).
{ECO:0000305}.
CONFLICT 183 183 E -> R (in Ref. 16; AAC03542).
{ECO:0000305}.
STRAND 89 94 {ECO:0000244|PDB:2E7A}.
STRAND 96 98 {ECO:0000244|PDB:2TUN}.
STRAND 99 101 {ECO:0000244|PDB:2E7A}.
STRAND 106 108 {ECO:0000244|PDB:1A8M}.
STRAND 112 114 {ECO:0000244|PDB:2E7A}.
STRAND 118 120 {ECO:0000244|PDB:2E7A}.
STRAND 123 125 {ECO:0000244|PDB:2E7A}.
STRAND 130 144 {ECO:0000244|PDB:2E7A}.
STRAND 146 148 {ECO:0000244|PDB:2ZPX}.
STRAND 152 159 {ECO:0000244|PDB:2E7A}.
HELIX 161 163 {ECO:0000244|PDB:2E7A}.
STRAND 167 174 {ECO:0000244|PDB:2E7A}.
STRAND 177 179 {ECO:0000244|PDB:1A8M}.
STRAND 182 185 {ECO:0000244|PDB:4TSV}.
STRAND 189 202 {ECO:0000244|PDB:2E7A}.
STRAND 207 213 {ECO:0000244|PDB:2E7A}.
HELIX 215 217 {ECO:0000244|PDB:2E7A}.
STRAND 221 223 {ECO:0000244|PDB:3IT8}.
STRAND 225 232 {ECO:0000244|PDB:2E7A}.
SEQUENCE 233 AA; 25644 MW; 3DF90F96C9031FFE CRC64;
MSTESMIRDV ELAEEALPKK TGGPQGSRRC LFLSLFSFLI VAGATTLFCL LHFGVIGPQR
EEFPRDLSLI SPLAQAVRSS SRTPSDKPVA HVVANPQAEG QLQWLNRRAN ALLANGVELR
DNQLVVPSEG LYLIYSQVLF KGQGCPSTHV LLTHTISRIA VSYQTKVNLL SAIKSPCQRE
TPEGAEAKPW YEPIYLGGVF QLEKGDRLSA EINRPDYLDF AESGQVYFGI IAL


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