Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)

 IKKB_MOUSE              Reviewed;         757 AA.
O88351; Q9R1J6;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-NOV-2018, entry version 174.
RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta;
Short=I-kappa-B-kinase beta;
Short=IKK-B;
Short=IKK-beta;
Short=IkBKB;
EC=2.7.11.10;
AltName: Full=I-kappa-B kinase 2;
Short=IKK2;
AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta;
Short=NFKBIKB;
Name=Ikbkb; Synonyms=Ikkb;
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], AND PHOSPHORYLATION BY MEKK1.
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=9520401; DOI=10.1073/pnas.95.7.3537;
Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H.,
Okumura K.;
"Differential regulation of IkappaB kinase alpha and beta by two
upstream kinases, NF-kappaB-inducing kinase and mitogen-activated
protein kinase/ERK kinase kinase-1.";
Proc. Natl. Acad. Sci. U.S.A. 95:3537-3542(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R.;
"Murine IkB kinase-B, a developmentally regulated protein kinase that
constitutively phosphorylates serine residues of IkB.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
DISRUPTION PHENOTYPE.
PubMed=10229185; DOI=10.1016/S1074-7613(00)80042-4;
Tanaka M., Fuentes M.E., Yamaguchi K., Durnin M.H., Dalrymple S.A.,
Hardy K.L., Goeddel D.V.;
"Embryonic lethality, liver degeneration, and impaired NF-kappa B
activation in IKK-beta-deficient mice.";
Immunity 10:421-429(1999).
[4]
DEVELOPMENTAL STAGE.
PubMed=10523828; DOI=10.1038/sj.onc.1202740;
Hu M.C.-T., Wang Y.-P., Qiu W.R., Mikhail A., Meyer C.F., Tan T.-H.;
"Hematopoietic progenitor kinase-1 (HPK1) stress response signaling
pathway activates IkappaB kinases (IKK-alpha/beta) and IKK-beta is a
developmentally regulated protein kinase.";
Oncogene 18:5514-5524(1999).
[5]
IKK PHOSPHORYLATION.
PubMed=9819420; DOI=10.1128/MCB.18.12.7336;
Nemoto S., DiDonato J.A., Lin A.;
"Coordinate regulation of IkappaB kinases by mitogen-activated protein
kinase kinase kinase 1 and NF-kappaB-inducing kinase.";
Mol. Cell. Biol. 18:7336-7343(1998).
[6]
DISRUPTION PHENOTYPE.
PubMed=10195897; DOI=10.1126/science.284.5412.321;
Li Q., Van Antwerp D., Mercurio F., Lee K.F., Verma I.M.;
"Severe liver degeneration in mice lacking the IkappaB kinase 2
gene.";
Science 284:321-325(1999).
[7]
REVIEW.
PubMed=10712233;
Jobin C., Sartor R.B.;
"The I kappa B/NF-kappa B system: a key determinant of mucosal
inflammation and protection.";
Am. J. Physiol. 278:C451-C462(2000).
[8]
INTERACTION WITH EIF2AK2.
PubMed=10848580; DOI=10.1128/MCB.20.13.4532-4542.2000;
Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.;
"PKR stimulates NF-kappaB irrespective of its kinase function by
interacting with the IkappaB kinase complex.";
Mol. Cell. Biol. 20:4532-4542(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
Testis;
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).
[10]
INTERACTION WITH TERF2IP.
PubMed=20622870; DOI=10.1038/ncb2080;
Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J.,
Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
"Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
dependent gene expression.";
Nat. Cell Biol. 12:758-767(2010).
[11]
INTERACTION WITH ZC3H12A.
PubMed=22037600; DOI=10.1038/ni.2137;
Iwasaki H., Takeuchi O., Teraguchi S., Matsushita K., Uehata T.,
Kuniyoshi K., Satoh T., Saitoh T., Matsushita M., Standley D.M.,
Akira S.;
"The IkappaB kinase complex regulates the stability of cytokine-
encoding mRNA induced by TLR-IL-1R by controlling degradation of
regnase-1.";
Nat. Immunol. 12:1167-1175(2011).
[12]
INTERACTION WITH AKAP13, IDENTIFICATION BY MASS SPECTROMETRY, AND
TISSUE SPECIFICITY.
PubMed=23090968; DOI=10.1128/MCB.00887-12;
del Vescovo C.D., Cotecchia S., Diviani D.;
"A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
interleukin-6-mediated cardiomyocyte hypertrophy.";
Mol. Cell. Biol. 33:14-27(2013).
-!- FUNCTION: Serine kinase that plays an essential role in the NF-
kappa-B signaling pathway which is activated by multiple stimuli
such as inflammatory cytokines, bacterial or viral products, DNA
damages or other cellular stresses. Acts as part of the canonical
IKK complex in the conventional pathway of NF-kappa-B activation
and phosphorylates inhibitors of NF-kappa-B on 2 critical serine
residues. These modifications allow polyubiquitination of the
inhibitors and subsequent degradation by the proteasome. In turn,
free NF-kappa-B is translocated into the nucleus and activates the
transcription of hundreds of genes involved in immune response,
growth control, or protection against apoptosis. In addition to
the NF-kappa-B inhibitors, phosphorylates several other components
of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits
RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE.
IKK-related kinase phosphorylations may prevent the overproduction
of inflammatory mediators since they exert a negative regulation
on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-
dependent inactivation of this pro-apoptotic transcription factor.
Also phosphorylates other substrates including NCOA3, BCL10 and
IRS1. Within the nucleus, acts as an adapter protein for NFKBIA
degradation in UV-induced NF-kappa-B activation.
{ECO:0000250|UniProtKB:O14920}.
-!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
phosphoprotein].
-!- SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex
consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-
beta/IKBKB dimers are associated with four gamma/IKBKG subunits.
The IKK core complex seems to associate with regulatory or adapter
proteins to form a IKK-signalosome holo-complex (By similarity).
The IKK complex associates with TERF2IP/RAP1, leading to promote
IKK-mediated phosphorylation of RELA/p65 (PubMed:20622870). Part
of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and
CREBBP. Part of a 70-90 kDa complex at least consisting of
CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14. Found in a
membrane raft complex, at least composed of BCL10, CARD11, DPP4
and IKBKB. Interacts with SQSTM1 through PRKCZ or PRKCI. Forms an
NGF-induced complex with IKBKB, PRKCI and TRAF6. May interact with
MAVS/IPS1. Interacts with NALP2. Interacts with TICAM1. Interacts
with FAF1; the interaction disrupts the IKK complex formation.
Interacts with ATM. Part of a ternary complex consisting of TANK,
IKBKB and IKBKG. Interacts with NIBP; the interaction is direct.
Interacts with ARRB1 and ARRB2. Interacts with TRIM21. Interacts
with NLRC5; prevents IKBKB phosphorylation and kinase activity.
Interacts with PDPK1 (By similarity). Interacts with EIF2AK2/PKR
(PubMed:10848580). The phosphorylated form interacts with PPM1A
and PPM1B. Interacts with ZNF268 isoform 2; the interaction is
further increased in a TNF-alpha-dependent manner. Interacts with
IKBKE. Interacts with NAA10, leading to NAA10 degradation.
Interacts with FOXO3 (By similarity). Interacts with ZC3H12A
(PubMed:22037600). Interacts with AKAP13 (PubMed:23090968).
Interacts with LRRC14; disrupts IKBKB-IKBKG interaction preventing
I-kappa-B-kinase (IKK) core complex formation and leading to a
decrease of IKBKB phosphorylation and NF-kappaB activation (By
similarity). {ECO:0000250|UniProtKB:O14920,
ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:20622870,
ECO:0000269|PubMed:22037600}.
-!- INTERACTION:
Q60680:Chuk; NbExp=4; IntAct=EBI-447960, EBI-646245;
O88522:Ikbkg; NbExp=7; IntAct=EBI-447960, EBI-998011;
Q14145:KEAP1 (xeno); NbExp=2; IntAct=EBI-447960, EBI-751001;
P68040:Rack1; NbExp=4; IntAct=EBI-447960, EBI-296749;
P01375:TNF (xeno); NbExp=3; IntAct=EBI-447960, EBI-359977;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14920}.
Nucleus {ECO:0000250|UniProtKB:O14920}. Membrane raft
{ECO:0000250|UniProtKB:O14920}. Note=Colocalized with DPP4 in
membrane rafts. {ECO:0000250|UniProtKB:O14920}.
-!- TISSUE SPECIFICITY: Detected in heart (at protein level)
(PubMed:23090968). Expressed in liver, kidney and spleen.
{ECO:0000269|PubMed:23090968}.
-!- DEVELOPMENTAL STAGE: While it is expressed ubiquitously throughout
the mouse embryo, at E9.5 day its expression begins to be
localized to the brain, neural ganglia, neural tube, and in liver
at E12.5 day. At E15.5 day, the expression is further restricted
to specific tissues of the embryo. {ECO:0000269|PubMed:10523828}.
-!- DOMAIN: The kinase domain is located in the N-terminal region. The
leucine zipper is important to allow homo- and hetero-
dimerization. At the C-terminal region is located the region
responsible for the interaction with NEMO/IKBKG (By similarity).
{ECO:0000250}.
-!- PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-
181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which
enhances activity. Once activated, autophosphorylates on the C-
terminal serine cluster; which decreases activity and prevents
prolonged activation of the inflammatory response. Phosphorylated
by the IKK-related kinases TBK1 and IKBKE, which is associated
with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent
gene transcription. Dephosphorylated at Ser-177 and Ser-181 by
PPM1A and PPM1B. {ECO:0000250|UniProtKB:O14920}.
-!- PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads
to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may
not serve as a monoubiquitination site. Ubiquitination on 'Ser-
163' may modulate phosphorylation on C-terminal serine residues.
{ECO:0000250|UniProtKB:O14920}.
-!- PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under
hypoxic conditions results in activation of NF-kappa-B.
{ECO:0000250|UniProtKB:O14920}.
-!- DISRUPTION PHENOTYPE: Mice present extensive liver damage from
apoptosis and die as embryos. They show a marked reduction in TNF-
alpha and IL1-alpha-induced NF-kappa-B activity.
{ECO:0000269|PubMed:10195897, ECO:0000269|PubMed:10229185}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. I-kappa-B kinase subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF026524; AAC23557.1; -; mRNA.
EMBL; AF088910; AAD52095.1; -; mRNA.
CCDS; CCDS52522.1; -.
RefSeq; NP_034676.1; NM_010546.2.
UniGene; Mm.277886; -.
ProteinModelPortal; O88351; -.
SMR; O88351; -.
BioGrid; 200601; 25.
ComplexPortal; CPX-3270; IkappaB kinase complex.
CORUM; O88351; -.
DIP; DIP-29813N; -.
IntAct; O88351; 26.
MINT; O88351; -.
STRING; 10090.ENSMUSP00000033939; -.
BindingDB; O88351; -.
ChEMBL; CHEMBL6012; -.
iPTMnet; O88351; -.
PhosphoSitePlus; O88351; -.
EPD; O88351; -.
MaxQB; O88351; -.
PaxDb; O88351; -.
PeptideAtlas; O88351; -.
PRIDE; O88351; -.
GeneID; 16150; -.
KEGG; mmu:16150; -.
CTD; 3551; -.
MGI; MGI:1338071; Ikbkb.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
HOGENOM; HOG000038048; -.
HOVERGEN; HBG018241; -.
InParanoid; O88351; -.
KO; K07209; -.
PhylomeDB; O88351; -.
BRENDA; 2.7.11.10; 3474.
PRO; PR:O88351; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_IKBKB; -.
GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; TAS:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0008385; C:IkappaB kinase complex; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008384; F:IkappaB kinase activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0007252; P:I-kappaB phosphorylation; TAS:MGI.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:2001259; P:positive regulation of cation channel activity; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0010765; P:positive regulation of sodium ion transport; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
InterPro; IPR022007; IKKbetaNEMObind.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12179; IKKbetaNEMObind; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM01239; IKKbetaNEMObind; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Hydroxylation;
Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; S-nitrosylation;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 757 Inhibitor of nuclear factor kappa-B
kinase subunit beta.
/FTId=PRO_0000086014.
DOMAIN 15 300 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 21 29 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 458 479 Leucine-zipper.
REGION 737 742 NEMO-binding.
ACT_SITE 145 145 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 177 177 Phosphoserine; by TBK1 and PKC/PRKCZ.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 179 179 S-nitrosocysteine.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 181 181 Phosphoserine; by TBK1, PKC/PRKCZ and
PDPK1. {ECO:0000250|UniProtKB:O14920}.
MOD_RES 191 191 Hydroxyproline. {ECO:0000250}.
MOD_RES 670 670 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 675 675 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 682 682 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 689 689 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 692 692 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 697 697 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 705 705 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 733 733 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 740 740 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14920}.
CONFLICT 56 56 N -> D (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 343 343 N -> D (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 356 356 K -> E (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 390 390 L -> F (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 406 406 P -> Q (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 573 573 K -> R (in Ref. 2; AAD52095).
{ECO:0000305}.
CONFLICT 736 757 TLDWSWLQMEDEERCSLEQACD -> VTA (in Ref.
2). {ECO:0000305}.
SEQUENCE 757 AA; 86690 MW; FED962F095449C5E CRC64;
MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQATGEQ IAIKQCRQEL SPKNRNRWCL
EIQIMRRLNH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ GGDLRRYLNQ FENCCGLREG
AVLTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEKRL IHKIIDLGYA KELDQGSLCT
SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE
VDIVVSEDLN GAVKFSSSLP FPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPQYGPNGCF
RALDDILNLK LVHVLNMVTG TVHTYPVTED ESLQSLKTRI QENTGILETD QELLQKAGLV
LLPDKPATQC ISDSKTNEGL TLDMDLVFLL DNSKINYETQ ITPRPPPESV SCILQEPKRN
LSFFQLRKVW GQVWHSIQTL KEDCNRLQQG QRAAMMSLLR NNSCLSKMKN AMASTAQQLK
AKLDFFKTSI QIDLEKYKEQ TEFGITSDKL LLAWREMEQA VEQCGRENDV KHLVERMMAL
QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRKLREKPRD QRTEGDSQEM VRLLLQAIQS
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE RTVVRLQEKR QKELWNLLKI
ACSKVRGPVS GSPDSMNVSR LSHPGQLMSQ PSSACDSLPE SDKKSEELVA EAHALCSRLE
SALQDTVKEQ DRSFTTLDWS WLQMEDEERC SLEQACD


Related products :

Catalog number Product name Quantity
U1953h CLIA Homo sapiens,Human,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKKB,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibito 96T
E1953h ELISA Homo sapiens,Human,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKKB,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibit 96T
U1953m CLIA I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,Mouse,Mus musculus,NFKBIKB,Nuclear factor NF-kappa-B inhibito 96T
U1953h CLIA kit Homo sapiens,Human,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKKB,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inh 96T
E1953m ELISA I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,Mouse,Mus musculus,NFKBIKB,Nuclear factor NF-kappa-B inhibit 96T
E1953h ELISA kit Homo sapiens,Human,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKKB,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B in 96T
U1953b CLIA Bos taurus,Bovine,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kina 96T
E1953b ELISA kit Bos taurus,Bovine,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibito 96T
E1953m ELISA kit I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,Mouse,Mus musculus,NFKBIKB,Nuclear factor NF-kappa-B in 96T
U1953m CLIA kit I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,Mouse,Mus musculus,NFKBIKB,Nuclear factor NF-kappa-B inh 96T
U1953b CLIA kit Bos taurus,Bovine,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor 96T
E1953b ELISA Bos taurus,Bovine,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kin 96T
E1953r ELISA kit I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kinase beta 96T
E1953r ELISA I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kinase beta,Rat, 96T
U1953r CLIA I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kinase beta,Rat,R 96T
U1953r CLIA kit I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,Ikbkb,IKK2,Ikkb,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor kinase beta, 96T
15-288-21171 Inhibitor of nuclear factor kappa B kinase subunit beta - EC 2.7.11.10; I-kappa-B-kinase beta; IkBKB; IKK-beta; IKK-B; I-kappa-B kinase 2; IKK2; Nuclear factor NF-kappa-B inhibitor kinase beta; NFKBIK 0.1 mg
18-661-15057 Inhibitor of nuclear factor kappa B kinase subunit beta - EC 2.7.11.10; I-kappa-B-kinase beta; IkBKB; IKK-beta; IKK-B; I-kappa-B kinase 2; IKK2; Nuclear factor NF-kappa-B inhibitor kinase beta; NFKBIK 0.1 mg
15-288-21171 Inhibitor of nuclear factor kappa B kinase subunit beta - EC 2.7.11.10; I-kappa-B-kinase beta; IkBKB; IKK-beta; IKK-B; I-kappa-B kinase 2; IKK2; Nuclear factor NF-kappa-B inhibitor kinase beta; NFKBIK 0.05 mg
CSB-EL011572RA Rat Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit 96T
CSB-EL011572RA Rat Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit SpeciesRat 96T
CSB-EL011572MO Mouse Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit 96T
CSB-EL011572BO Bovine Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit 96T
CSB-EL011572MO Mouse Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit SpeciesMouse 96T
CSB-EL011572BO Bovine Inhibitor of nuclear factor kappa-B kinase subunit beta(IKBKB) ELISA kit SpeciesBovine 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur