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Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]

 NFKB1_MOUSE             Reviewed;         971 AA.
P25799; B2RRQ6; Q3TZE8; Q3V2V6; Q6TDG8; Q75ZL1; Q80Y21; Q8C712;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 201.
RecName: Full=Nuclear factor NF-kappa-B p105 subunit;
AltName: Full=DNA-binding factor KBF1;
AltName: Full=EBP-1;
AltName: Full=NF-kappa-B1 p84/NF-kappa-B1 p98;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1;
Contains:
RecName: Full=Nuclear factor NF-kappa-B p50 subunit;
Name=Nfkb1;
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 [MRNA] (ISOFORM 1).
TISSUE=Lung, and Spleen;
PubMed=2203532; DOI=10.1016/0092-8674(90)90276-K;
Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P.,
Baltimore D.;
"Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel
and dorsal.";
Cell 62:1019-1029(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
PubMed=1339305; DOI=10.1016/0092-8674(92)90082-N;
Inoue J., Kerr L.D., Kakizuka A., Verma I.M.;
"I kappa B gamma, a 70 kd protein identical to the C-terminal half of
p110 NF-kappa B: a new member of the I kappa B family.";
Cell 68:1109-1120(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE.
PubMed=8398903;
Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J.,
Grumont R.J.;
"The activity of a 70 kilodalton I kappa B molecule identical to the
carboxyl terminus of the p105 NF-kappa B precursor is modulated by
protein kinase A.";
Cell Growth Differ. 4:617-627(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
PubMed=7969179; DOI=10.1128/MCB.14.12.8460;
Grumont R.J., Fecondo J., Gerondakis S.;
"Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of
the p50 precursor NF-kappa B1 that can function as a transactivator of
NF-kappa B-regulated transcription.";
Mol. Cell. Biol. 14:8460-8470(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6CrSlc; TISSUE=Spleen;
Ohara O., Kitamura H., Nakagawa T.;
"Mus musculus transcription factor NF-kappa-B DNA binding
subunit(p105) mRNA, complete cds.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C3H/HeJBir, and C57BL/6J;
Bleich A., Hedrich H.J., Schlegelberger B., Maehler M.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Brain, and Embryo;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 54-129.
STRAIN=C57BL/6J; TISSUE=Lung carcinoma;
Gerhauser I., Ulrich R., Baumgartner W.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Kidney, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[11]
ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), AND SUBCELLULAR LOCATION.
PubMed=8183915; DOI=10.1073/pnas.91.10.4367;
Grumont R.J., Gerondakis S.;
"Alternative splicing of RNA transcripts encoded by the murine p105
NF-kappa B gene generates I kappa B gamma isoforms with different
inhibitory activities.";
Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994).
[12]
COTRANSLATIONAL FOLDING OF P105.
PubMed=9529257; DOI=10.1016/S0092-8674(00)81409-9;
Lin L., DeMartino G.N., Greene W.C.;
"Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome.";
Cell 92:819-828(1998).
[13]
INTERACTION WITH NFKBIZ.
PubMed=11356851; DOI=10.1074/jbc.M103426200;
Yamazaki S., Muta T., Takeshige K.;
"A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory
stimuli, negatively regulates nuclear factor-kappaB in the nuclei.";
J. Biol. Chem. 276:27657-27662(2001).
[14]
INTERACTION WITH NFKBID.
PubMed=11931770; DOI=10.1016/S1097-2765(02)00469-0;
Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M.,
Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M.,
Reinherz E.L., Clayton L.K.;
"Peptide-induced negative selection of thymocytes activates
transcription of an NF-kappa B inhibitor.";
Mol. Cell 9:637-648(2002).
[15]
IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
PubMed=15051764; DOI=10.1084/jem.20031272;
Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D.,
Willems F., Goldman M.;
"A defect in nucleosome remodeling prevents IL-12(p35) gene
transcription in neonatal dendritic cells.";
J. Exp. Med. 199:1011-1016(2004).
[16]
INTERACTION WITH NFKBIZ.
PubMed=15241416; DOI=10.1038/nature02738;
Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K.,
Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T.,
Yamaoka S., Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.;
"Regulation of Toll/IL-1-receptor-mediated gene expression by the
inducible nuclear protein IkappaBzeta.";
Nature 430:218-222(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-940 AND
THR-946, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364.
PubMed=7530332; DOI=10.1038/373303a0;
Ghosh G., van Duyne G., Ghosh S., Sigler P.B.;
"Structure of NF-kappa B p50 homodimer bound to a kappa B site.";
Nature 373:303-310(1995).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350.
PubMed=9384558; DOI=10.1016/S0969-2126(97)00293-1;
Huang D.B., Huxford T., Chen Y.Q., Ghosh G.;
"The role of DNA in the mechanism of NFkappaB dimer formation: crystal
structures of the dimerization domains of the p50 and p65 subunits.";
Structure 5:1427-1436(1997).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363.
PubMed=9865694; DOI=10.1016/S0092-8674(00)81699-2;
Huxford T., Huang D.B., Malek S., Ghosh G.;
"The crystal structure of the IkappaBalpha/NF-kappaB complex reveals
mechanisms of NF-kappaB inactivation.";
Cell 95:759-770(1998).
[21]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350.
PubMed=9450761; DOI=10.1038/34956;
Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.;
"Crystal structure of p50/p65 heterodimer of transcription factor NF-
kappaB bound to DNA.";
Nature 391:410-413(1998).
[22]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350.
PubMed=11970948; DOI=10.1074/jbc.M200006200;
Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G.;
"The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer
bound to the interferon beta -kappa B site.";
J. Biol. Chem. 277:24694-24700(2002).
[23]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350.
PubMed=11970949; DOI=10.1074/jbc.M200007200;
Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G.;
"The kappa B DNA sequence from the HIV long terminal repeat functions
as an allosteric regulator of HIV transcription.";
J. Biol. Chem. 277:24701-24708(2002).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED
WITH RNA APTAMER.
PubMed=12886018; DOI=10.1073/pnas.1632011100;
Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III,
Ghosh G.;
"Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity
RNA aptamer.";
Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003).
[25]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB.
PubMed=17869269; DOI=10.1016/j.jmb.2007.08.039;
Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.;
"X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly
of multiple dimers on tandem kappaB sites.";
J. Mol. Biol. 373:723-734(2007).
-!- FUNCTION: NF-kappa-B is a pleiotropic transcription factor present
in almost all cell types and is the endpoint of a series of signal
transduction events that are initiated by a vast array of stimuli
related to many biological processes such as inflammation,
immunity, differentiation, cell growth, tumorigenesis and
apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed
by the Rel-like domain-containing proteins RELA/p65, RELB,
NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric
p65-p50 complex appears to be most abundant one. The dimers bind
at kappa-B sites in the DNA of their target genes and the
individual dimers have distinct preferences for different kappa-B
sites that they can bind with distinguishable affinity and
specificity. Different dimer combinations act as transcriptional
activators or repressors, respectively. NF-kappa-B is controlled
by various mechanisms of post-translational modification and
subcellular compartmentalization as well as by interactions with
other cofactors or corepressors. NF-kappa-B complexes are held in
the cytoplasm in an inactive state complexed with members of the
NF-kappa-B inhibitor (I-kappa-B) family. In a conventional
activation pathway, I-kappa-B is phosphorylated by I-kappa-B
kinases (IKKs) in response to different activators, subsequently
degraded thus liberating the active NF-kappa-B complex which
translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and
RelB-p50 complexes are transcriptional activators. The NF-kappa-B
p50-p50 homodimer is a transcriptional repressor, but can act as a
transcriptional activator when associated with BCL3. NFKB1 appears
to have dual functions such as cytoplasmic retention of attached
NF-kappa-B proteins by p105 and generation of p50 by a
cotranslational processing. The proteasome-mediated process
ensures the production of both p50 and p105 and preserves their
independent function, although processing of NFKB1/p105 also
appears to occur post-translationally. p50 binds to the kappa-B
consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region
of genes involved in immune response and acute phase reactions.
Plays a role in the regulation of apoptosis. Isoform 5, isoform 6
and isoform 7 act as inhibitors of transactivation of p50 NF-
kappa-B subunit, probably by sequestering it in the cytoplasm.
Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of
NF-kappa-B-regulated gene expression. In a complex with MAP3K8,
NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8
is released by proteasome-dependent degradation of NFKB1/p105.
-!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of
the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-
kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50
complex. Component of the NF-kappa-B p50-c-Rel complex. Component
of a complex consisting of the NF-kappa-B p50-p50 homodimer and
BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts
with NCOA3 coactivator, which may coactivate NF-kappa-B dependent
expression via its histone acetyltransferase activity. Interacts
with DSIPI; this interaction prevents nuclear translocation and
DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts
with CFLAR; the interaction inhibits p105 processing into p50.
NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2.
Interacts with GSK3B; the interaction prevents processing of p105
to p50. NFKB1/p50 interacts with NFKBIE (By similarity). NFKB1/p50
interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit
interacts with NFKBID. Directly interacts with MEN1 (By
similarity). Interacts with HIF1AN (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9DBR0:Akap8; NbExp=4; IntAct=EBI-643958, EBI-4285802;
Q3V096:Ankrd42; NbExp=3; IntAct=EBI-1209141, EBI-15861272;
O09106:Hdac1; NbExp=2; IntAct=EBI-643958, EBI-301912;
Q15788:NCOA1 (xeno); NbExp=2; IntAct=EBI-643958, EBI-455189;
Q04207:Rela; NbExp=6; IntAct=EBI-643974, EBI-644400;
Q04863:Relb; NbExp=2; IntAct=EBI-1209141, EBI-1209145;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, but also
found in the cytoplasm in an inactive form complexed to an
inhibitor (I-kappa-B).
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 6: Nucleus. Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 7: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=p105;
IsoId=P25799-1; Sequence=Displayed;
Name=2; Synonyms=p84;
IsoId=P25799-2; Sequence=VSP_005583;
Name=3; Synonyms=p98;
IsoId=P25799-3; Sequence=VSP_005584;
Name=4;
IsoId=P25799-4; Sequence=VSP_017237, VSP_017238;
Name=5; Synonyms=P70, I-kappa-B gamma;
IsoId=P25799-5; Sequence=VSP_017236;
Name=6; Synonyms=p63, I-kappa-B gamma-1;
IsoId=P25799-6; Sequence=VSP_017236, VSP_005584;
Name=7; Synonyms=p55, I-kappa-B gamma-2;
IsoId=P25799-7; Sequence=VSP_017236, VSP_005583;
Note=Inhibits the activity of the p50 NF-kappa-B subunit.;
-!- INDUCTION: By phorbol ester and TNF-alpha.
-!- DOMAIN: The C-terminus of p105 might be involved in cytoplasmic
retention, inhibition of DNA-binding, and transcription
activation.
-!- DOMAIN: Glycine-rich region (GRR) appears to be a critical element
in the generation of p50.
-!- PTM: While translation occurs, the particular unfolded structure
after the GRR repeat promotes the generation of p50 making it an
acceptable substrate for the proteasome. This process is known as
cotranslational processing. The processed form is active and the
unprocessed form acts as an inhibitor (I kappa B-like), being able
to form cytosolic complexes with NF-kappa B, trapping it in the
cytoplasm. Complete folding of the region downstream of the GRR
repeat precludes processing.
-!- PTM: Phosphorylation at 'Ser-930' and 'Ser-935' are required for
BTRC/BTRCP-mediated proteolysis. {ECO:0000250}.
-!- PTM: Polyubiquitination seems to allow p105 processing.
-!- PTM: S-nitrosylation of Cys-59 affects DNA binding. {ECO:0000250}.
-!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
prostaglandin-J2 is autocatalytic and reversible. It may occur as
an alternative to other cysteine modifications, such as S-
nitrosylation and S-palmitoylation (By similarity). {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAC35117.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M57999; AAA40415.1; -; mRNA.
EMBL; S89033; AAB21851.1; -; mRNA.
EMBL; S66656; AAB28573.1; -; mRNA.
EMBL; AB119195; BAC84979.1; -; mRNA.
EMBL; AY521462; AAS00547.1; -; mRNA.
EMBL; AY521463; AAS00548.1; -; mRNA.
EMBL; CH466532; EDL12143.1; -; Genomic_DNA.
EMBL; BC050841; AAH50841.1; -; mRNA.
EMBL; BC138535; AAI38536.1; -; mRNA.
EMBL; BC138536; AAI38537.1; -; mRNA.
EMBL; AY423849; AAR00341.1; -; mRNA.
EMBL; AK052726; BAC35117.1; ALT_INIT; mRNA.
EMBL; AK089660; BAE43399.1; -; mRNA.
EMBL; AK157915; BAE34261.1; -; mRNA.
CCDS; CCDS17858.1; -. [P25799-1]
PIR; A35697; A35697.
RefSeq; NP_032715.2; NM_008689.2. [P25799-1]
RefSeq; XP_006501169.1; XM_006501106.2. [P25799-3]
UniGene; Mm.256765; -.
PDB; 1BFS; X-ray; 2.20 A; A=245-350.
PDB; 1IKN; X-ray; 2.30 A; C=245-363.
PDB; 1LE5; X-ray; 2.75 A; B/F=39-350.
PDB; 1LE9; X-ray; 3.00 A; B/F=39-350.
PDB; 1LEI; X-ray; 2.70 A; B=39-350.
PDB; 1NFK; X-ray; 2.30 A; A/B=39-363.
PDB; 1OOA; X-ray; 2.45 A; A/B=39-363.
PDB; 1U36; X-ray; 1.89 A; A=245-350.
PDB; 1U3J; X-ray; 1.90 A; A=245-350.
PDB; 1U3Y; X-ray; 1.90 A; A=245-350.
PDB; 1U3Z; X-ray; 1.90 A; A=245-350.
PDB; 1U41; X-ray; 2.20 A; A/B/C/D=245-350.
PDB; 1U42; X-ray; 2.70 A; A=245-350.
PDB; 1VKX; X-ray; 2.90 A; B=39-350.
PDB; 2I9T; X-ray; 2.80 A; B=39-350.
PDB; 2V2T; X-ray; 3.05 A; B=38-363.
PDB; 3JV4; X-ray; 3.15 A; B/D/F=245-359.
PDBsum; 1BFS; -.
PDBsum; 1IKN; -.
PDBsum; 1LE5; -.
PDBsum; 1LE9; -.
PDBsum; 1LEI; -.
PDBsum; 1NFK; -.
PDBsum; 1OOA; -.
PDBsum; 1U36; -.
PDBsum; 1U3J; -.
PDBsum; 1U3Y; -.
PDBsum; 1U3Z; -.
PDBsum; 1U41; -.
PDBsum; 1U42; -.
PDBsum; 1VKX; -.
PDBsum; 2I9T; -.
PDBsum; 2V2T; -.
PDBsum; 3JV4; -.
ProteinModelPortal; P25799; -.
SMR; P25799; -.
BioGrid; 201751; 13.
CORUM; P25799; -.
DIP; DIP-85N; -.
IntAct; P25799; 20.
MINT; MINT-236136; -.
STRING; 10090.ENSMUSP00000029812; -.
ChEMBL; CHEMBL1949489; -.
iPTMnet; P25799; -.
PhosphoSitePlus; P25799; -.
EPD; P25799; -.
MaxQB; P25799; -.
PaxDb; P25799; -.
PeptideAtlas; P25799; -.
PRIDE; P25799; -.
Ensembl; ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
Ensembl; ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
GeneID; 18033; -.
KEGG; mmu:18033; -.
UCSC; uc008rlw.1; mouse. [P25799-1]
UCSC; uc008rly.1; mouse. [P25799-4]
UCSC; uc012cyf.1; mouse. [P25799-6]
CTD; 4790; -.
MGI; MGI:97312; Nfkb1.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00500000044765; -.
HOVERGEN; HBG052613; -.
InParanoid; P25799; -.
KO; K02580; -.
OMA; PFRYKPR; -.
OrthoDB; EOG091G03PF; -.
TreeFam; TF325632; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-209560; NF-kB is activated and signals survival.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-446652; Interleukin-1 family signaling.
Reactome; R-MMU-448706; Interleukin-1 processing.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; Nfkb1; mouse.
EvolutionaryTrace; P25799; -.
PRO; PR:P25799; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028163; -.
ExpressionAtlas; P25799; baseline and differential.
Genevisible; P25799; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0042805; F:actinin binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0000975; F:regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0071359; P:cellular response to dsRNA; IMP:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0048535; P:lymph node development; TAS:MGI.
GO; GO:0010956; P:negative regulation of calcidiol 1-monooxygenase activity; ISO:MGI.
GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
GO; GO:0045083; P:negative regulation of interleukin-12 biosynthetic process; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISO:MGI.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
CDD; cd00204; ANK; 1.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 1.25.40.20; -; 3.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR030503; NF-kB_p105.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF9; PTHR24169:SF9; 1.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00531; Death; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00248; ANK; 6.
SMART; SM00005; DEATH; 1.
SMART; SM00429; IPT; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ANK repeat; Apoptosis; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Hydroxylation;
Isopeptide bond; Lipoprotein; Nucleus; Phosphoprotein;
Reference proteome; Repeat; S-nitrosylation; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 971 Nuclear factor NF-kappa-B p105 subunit.
/FTId=PRO_0000030312.
CHAIN 1 431 Nuclear factor NF-kappa-B p50 subunit.
{ECO:0000250}.
/FTId=PRO_0000030313.
DOMAIN 40 365 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
REPEAT 538 567 ANK 1.
REPEAT 577 606 ANK 2.
REPEAT 610 639 ANK 3.
REPEAT 646 675 ANK 4.
REPEAT 680 710 ANK 5.
REPEAT 714 743 ANK 6.
REPEAT 767 797 ANK 7.
DOMAIN 801 888 Death.
REGION 370 392 GRR.
REGION 433 971 Interaction with CFLAR. {ECO:0000250}.
REGION 646 680 Essential for interaction with HIF1AN.
{ECO:0000250}.
MOTIF 358 363 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 373 431 Gly-rich.
SITE 431 432 Cleavage (when cotranslationally
processed). {ECO:0000250}.
MOD_RES 59 59 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 335 335 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 438 438 N6-acetyllysine; by EP300. {ECO:0000250}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 674 674 (3S)-3-hydroxyasparagine; by HIF1AN.
{ECO:0000250}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000250|UniProtKB:Q63369}.
MOD_RES 896 896 Phosphoserine.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 910 910 Phosphoserine; by GSK3-beta; in vitro.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 930 930 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 935 935 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:P19838}.
MOD_RES 940 940 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 946 946 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
LIPID 59 59 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine; alternate. {ECO:0000250}.
CROSSLNK 323 323 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P19838}.
VAR_SEQ 1 364 Missing (in isoform 5, isoform 6 and
isoform 7). {ECO:0000303|PubMed:1339305,
ECO:0000303|PubMed:8398903}.
/FTId=VSP_017236.
VAR_SEQ 353 356 DKEE -> GTWV (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_017237.
VAR_SEQ 357 971 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_017238.
VAR_SEQ 780 971 VFDILNGKPYEPVFTSDDILPQGDMKQLTEDTRLQLCKLLE
IPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVS
GGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVTTA
QVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSFTE
SLTGDSPLLSLNKMPHGYGQEGPIEGKI -> GT (in
isoform 2 and isoform 7).
{ECO:0000303|PubMed:7969179}.
/FTId=VSP_005583.
VAR_SEQ 860 971 VSGGTIKELMEALQQMGYTEAIEVIQAAFRTPATTASSPVT
TAQVHCLPLSSSSTRQHIDELRDSDSVCDSGVETSFRKLSF
TESLTGDSPLLSLNKMPHGYGQEGPIEGKI -> MNSGIVT
ASVTVVWRHPSANSALQSLLLETAHCYL (in isoform
3 and isoform 6).
{ECO:0000303|PubMed:7969179}.
/FTId=VSP_005584.
CONFLICT 111 111 L -> P (in Ref. 9; AAR00341).
{ECO:0000305}.
CONFLICT 265 265 E -> G (in Ref. 10; BAC35117).
{ECO:0000305}.
CONFLICT 530 530 H -> D (in Ref. 10; BAE34261).
{ECO:0000305}.
CONFLICT 546 546 A -> G (in Ref. 10; BAE34261).
{ECO:0000305}.
CONFLICT 684 684 A -> P (in Ref. 1; AAA40415, 2; AAB21851
and 3; AAB28573). {ECO:0000305}.
CONFLICT 732 732 A -> T (in Ref. 10; BAE34261).
{ECO:0000305}.
CONFLICT 950 950 P -> A (in Ref. 10; BAE43399).
{ECO:0000305}.
STRAND 41 46 {ECO:0000244|PDB:1NFK}.
STRAND 50 52 {ECO:0000244|PDB:1NFK}.
HELIX 58 60 {ECO:0000244|PDB:1NFK}.
STRAND 62 64 {ECO:0000244|PDB:1VKX}.
STRAND 74 76 {ECO:0000244|PDB:1OOA}.
STRAND 81 85 {ECO:0000244|PDB:1NFK}.
STRAND 92 98 {ECO:0000244|PDB:1NFK}.
STRAND 100 103 {ECO:0000244|PDB:1NFK}.
STRAND 108 113 {ECO:0000244|PDB:1NFK}.
STRAND 117 119 {ECO:0000244|PDB:1LE9}.
STRAND 120 124 {ECO:0000244|PDB:1NFK}.
STRAND 131 133 {ECO:0000244|PDB:1NFK}.
STRAND 138 140 {ECO:0000244|PDB:1NFK}.
HELIX 144 146 {ECO:0000244|PDB:1OOA}.
HELIX 147 160 {ECO:0000244|PDB:1NFK}.
STRAND 162 164 {ECO:0000244|PDB:1VKX}.
HELIX 165 169 {ECO:0000244|PDB:1NFK}.
HELIX 171 173 {ECO:0000244|PDB:1OOA}.
STRAND 179 182 {ECO:0000244|PDB:1NFK}.
HELIX 188 203 {ECO:0000244|PDB:1NFK}.
STRAND 209 219 {ECO:0000244|PDB:1NFK}.
STRAND 221 223 {ECO:0000244|PDB:1NFK}.
STRAND 225 228 {ECO:0000244|PDB:1NFK}.
STRAND 232 239 {ECO:0000244|PDB:1OOA}.
STRAND 240 242 {ECO:0000244|PDB:1VKX}.
TURN 243 246 {ECO:0000244|PDB:1OOA}.
STRAND 250 254 {ECO:0000244|PDB:1U36}.
STRAND 256 259 {ECO:0000244|PDB:1U36}.
STRAND 265 271 {ECO:0000244|PDB:1U36}.
TURN 275 277 {ECO:0000244|PDB:1NFK}.
STRAND 279 284 {ECO:0000244|PDB:1U36}.
HELIX 287 289 {ECO:0000244|PDB:1BFS}.
STRAND 292 295 {ECO:0000244|PDB:1U36}.
HELIX 300 302 {ECO:0000244|PDB:1U36}.
TURN 305 307 {ECO:0000244|PDB:1U36}.
STRAND 308 312 {ECO:0000244|PDB:1U36}.
STRAND 325 332 {ECO:0000244|PDB:1U36}.
TURN 334 336 {ECO:0000244|PDB:1U36}.
STRAND 343 348 {ECO:0000244|PDB:1U36}.
STRAND 351 354 {ECO:0000244|PDB:1IKN}.
SEQUENCE 971 AA; 105615 MW; 91EA9C595E375C30 CRC64;
MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE
GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV
CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG
GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS
KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP
TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK
RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG
VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA
STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD
SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV
GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL
PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH
IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV
FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL
NNAFRLSPAP SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT
TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP LLSLNKMPHG
YGQEGPIEGK I


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