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Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)

 NFAC2_MOUSE             Reviewed;         927 AA.
Q60591; A2APK2; A2APK3; A2AQC5; A2AQC6; A2AQC7; B5B2Q3; Q60984;
Q60985; Q91Y65;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 173.
RecName: Full=Nuclear factor of activated T-cells, cytoplasmic 2;
Short=NF-ATc2;
Short=NFATc2;
AltName: Full=NFAT pre-existing subunit;
Short=NF-ATp;
AltName: Full=T-cell transcription factor NFAT1;
Name=Nfatc2; Synonyms=Nfat1, Nfatp;
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 PARTIAL PROTEIN SEQUENCE (ISOFORM A).
PubMed=8235597; DOI=10.1126/science.8235597;
McCaffrey P.G., Luo C., Kerpolla T.K., Jain J., Badalian T.M.,
Ho A.M., Burgeon E., Lane W.S., Lambert J.N., Curran T., Verdine G.L.,
Rao A., Hogan P.G.;
"Isolation of the cyclosporin-sensitive T cell transcription factor
NFATp.";
Science 262:750-754(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
PubMed=8668213; DOI=10.1128/MCB.16.7.3955;
Luo C., Burgeon E., Carew J.A., McCaffrey P.G., Badalian T.M.,
Lane W.S., Hogan P.G., Rao A.;
"Recombinant NFAT1 (NFATp) is regulated by calcineurin in T cells and
mediates transcription of several cytokine genes.";
Mol. Cell. Biol. 16:3955-3966(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=11278367; DOI=10.1074/jbc.M007854200;
Plyte S., Boncristiano M., Fattori E., Galvagni F., Paccani S.R.,
Majolini M.B., Oliviero S., Ciliberto G., Telford J.L., Baldari C.T.;
"Identification and characterization of a novel nuclear factor of
activated T-cells-1 isoform expressed in mouse brain.";
J. Biol. Chem. 276:14350-14358(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=18675896; DOI=10.1016/j.ygeno.2008.06.011;
Vihma H., Pruunsild P., Timmusk T.;
"Alternative splicing and expression of human and mouse NFAT genes.";
Genomics 92:279-291(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
MUTAGENESIS OF ARG-423; HIS-425; TYR-426; THR-428 AND GLU-429.
PubMed=7876165; DOI=10.1074/jbc.270.28.16854;
Jain J., Burgeon E., Badalian T.M., Hogan P.G., Rao A.;
"A similar DNA-binding motif in NFAT family proteins and the Rel
homology region.";
J. Biol. Chem. 270:4138-4145(1995).
[7]
INTERACTION WITH NFATC2IP.
PubMed=8943202; DOI=10.1126/science.274.5294.1903;
Hodge M.R., Chun H.J., Rengarajan J., Alt A., Lieberson R.,
Glimcher L.H.;
"NF-AT-driven interleukin-4 transcription potentiated by NIP45.";
Science 274:1903-1905(1996).
[8]
MUTAGENESIS OF ARG-112; GLU-114 AND THR-116.
PubMed=9660947; DOI=10.1016/S1097-2765(00)80063-5;
Aramburu J., Garcia-Cozar F., Raghavan A., Okamura H., Rao A.,
Hogan P.G.;
"Selective inhibition of NFAT activation by a peptide spanning the
calcineurin targeting site of NFAT.";
Mol. Cell 1:627-637(1998).
[9]
REVIEW.
PubMed=10089876; DOI=10.1016/S0092-8674(00)80571-1;
Crabtree G.R.;
"Generic signals and specific outcomes: signaling through Ca2+,
calcineurin, and NF-AT.";
Cell 96:611-614(1999).
[10]
PHOSPHORYLATION AT SER-99; SER-136; SER-170; SER-173; SER-174;
SER-176; SER-177; SER-179; SER-182; SER-215; SER-219; SER-223;
SER-238; SER-245; SER-270; SER-276; SER-278; SER-282; SER-328 AND
SER-365, SUBCELLULAR LOCATION, INTERACTION WITH XPO1, MUTAGENESIS OF
ARG-164, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11030334; DOI=10.1016/S1097-2765(00)00053-8;
Okamura H., Aramburu J., Garcia-Rodriguez C., Viola J.P.B.,
Raghavan A., Tahiliani M., Zhang X., Qin J., Hogan P.G., Rao A.;
"Concerted dephosphorylation of the transcription factor NFAT1 induces
a conformational switch that regulates transcriptional activity.";
Mol. Cell 6:539-550(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-257 AND
SER-365, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, 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).
[12]
INTERACTION WITH TBX21.
PubMed=23616576; DOI=10.4049/jimmunol.1203403;
Jang E.J., Park H.R., Hong J.H., Hwang E.S.;
"Lysine 313 of T-box is crucial for modulation of protein stability,
DNA binding, and threonine phosphorylation of T-bet.";
J. Immunol. 190:5764-5770(2013).
-!- FUNCTION: Plays a role in the inducible expression of cytokine
genes in T-cells, especially in the induction of the IL-2, IL-3,
IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the
activation of GPC6 expression and WNT5A signaling pathway.
{ECO:0000250|UniProtKB:Q13469}.
-!- SUBUNIT: Member of the multicomponent NFATC transcription complex
that consists of at least two components, a pre-existing
cytoplasmic component NFATC2 and an inducible nuclear component
NFATC1. Other members such as NFATC4, NFATC3 or members of the
activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind
the complex. The phosphorylated form specifically interacts with
XPO1; which mediates nuclear export. NFATC proteins bind to DNA as
monomers. Interacts with NFATC2IP. Interacts with FOXP3 (By
similarity). Interacts with TBX21 ('Thr-302' phosphorylated form)
(PubMed:23616576). {ECO:0000250|UniProtKB:Q13469,
ECO:0000269|PubMed:11030334, ECO:0000269|PubMed:23616576,
ECO:0000269|PubMed:8943202}.
-!- INTERACTION:
Q86Y07-1:VRK2 (xeno); NbExp=2; IntAct=EBI-643104, EBI-1207633;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11030334}.
Nucleus {ECO:0000269|PubMed:11030334}. Note=Cytoplasmic for the
phosphorylated form and nuclear after activation that is
controlled by calcineurin-mediated dephosphorylation. Rapid
nuclear exit of NFATC is thought to be one mechanism by which
cells distinguish between sustained and transient calcium signals.
The subcellular localization of NFATC plays a key role in the
regulation of gene transcription.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=C;
IsoId=Q60591-3; Sequence=Displayed;
Name=B;
IsoId=Q60591-2; Sequence=VSP_005596;
Name=D;
IsoId=Q60591-4; Sequence=VSP_005597;
Name=A;
IsoId=Q60591-1; Sequence=Not described;
Note=Ref.2 (AAC52929) sequence is a chimeric cDNA.;
-!- TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, testis,
brain, placenta, muscle and pancreas.
{ECO:0000269|PubMed:18675896}.
-!- DOMAIN: Rel Similarity Domain (RSD) allows DNA-binding and
cooperative interactions with AP1 factors. {ECO:0000250}.
-!- PTM: In resting cells, phosphorylated by NFATC-kinase on at least
18 sites in the 99-365 region. Upon cell stimulation, all these
sites except Ser-245 are dephosphorylated by calcineurin.
Dephosphorylation induces a conformational change that
simultaneously exposes an NLS and masks an NES, which results in
nuclear localization. Simultaneously, one site among Ser-53; Ser-
54 and Ser-56 is phosphorylated; which is required for full
transcriptional activity. {ECO:0000269|PubMed:11030334}.
-!- PTM: Ubiquitinated in endothelial cells by RNF213 downstream of
the non-canonical Wnt signaling pathway, leading to its
degradation by the proteasome. {ECO:0000250|UniProtKB:Q13469}.
-!- SEQUENCE CAUTION:
Sequence=AAC52929.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA fused with Phyhd1 (Lrrc8a).; Evidence={ECO:0000305};
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EMBL; U02079; AAC52929.1; ALT_SEQ; mRNA.
EMBL; U36575; AAC52930.1; -; mRNA.
EMBL; U36576; AAC52931.1; -; mRNA.
EMBL; AF289078; AAK49895.1; -; mRNA.
EMBL; EU887588; ACG55608.1; -; mRNA.
EMBL; AL840639; CAM15662.1; -; Genomic_DNA.
EMBL; AL844575; CAM15662.1; JOINED; Genomic_DNA.
EMBL; AL840639; CAM15663.1; -; Genomic_DNA.
EMBL; AL844575; CAM15663.1; JOINED; Genomic_DNA.
EMBL; AL844575; CAM15669.1; -; Genomic_DNA.
EMBL; AL844575; CAM15670.1; -; Genomic_DNA.
EMBL; AL840639; CAM15670.1; JOINED; Genomic_DNA.
EMBL; AL844575; CAM15671.1; -; Genomic_DNA.
EMBL; AL840639; CAM15671.1; JOINED; Genomic_DNA.
CCDS; CCDS17112.1; -. [Q60591-3]
CCDS; CCDS50803.1; -. [Q60591-2]
PIR; A48753; A48753.
RefSeq; NP_035029.2; NM_010899.3. [Q60591-3]
UniGene; Mm.116802; -.
ProteinModelPortal; Q60591; -.
SMR; Q60591; -.
BioGrid; 201739; 2.
CORUM; Q60591; -.
DIP; DIP-49476N; -.
ELM; Q60591; -.
IntAct; Q60591; 11.
MINT; MINT-1565857; -.
STRING; 10090.ENSMUSP00000074198; -.
iPTMnet; Q60591; -.
PhosphoSitePlus; Q60591; -.
EPD; Q60591; -.
PaxDb; Q60591; -.
PeptideAtlas; Q60591; -.
PRIDE; Q60591; -.
Ensembl; ENSMUST00000074618; ENSMUSP00000074198; ENSMUSG00000027544. [Q60591-3]
Ensembl; ENSMUST00000109184; ENSMUSP00000104812; ENSMUSG00000027544. [Q60591-2]
GeneID; 18019; -.
KEGG; mmu:18019; -.
UCSC; uc008oau.2; mouse. [Q60591-3]
CTD; 4773; -.
MGI; MGI:102463; Nfatc2.
eggNOG; ENOG410IHFR; Eukaryota.
eggNOG; ENOG41105U2; LUCA.
GeneTree; ENSGT00550000074562; -.
HOVERGEN; HBG069754; -.
InParanoid; Q60591; -.
KO; K17332; -.
OMA; MWKTSPD; -.
OrthoDB; EOG091G01QP; -.
TreeFam; TF326480; -.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
ChiTaRS; Nfatc2; mouse.
PRO; PR:Q60591; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027544; -.
ExpressionAtlas; Q60591; baseline and differential.
Genevisible; Q60591; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IGI:MGI.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0001816; P:cytokine production; IDA:MGI.
GO; GO:0014904; P:myotube cell development; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IMP: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; ISO:MGI.
GO; GO:0042493; P:response to drug; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR008366; NFAT.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
InterPro; IPR037059; RHD_DNA_bind_dom_sf.
PANTHER; PTHR12533; PTHR12533; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR01789; NUCFACTORATC.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 927 Nuclear factor of activated T-cells,
cytoplasmic 2.
/FTId=PRO_0000205179.
REPEAT 186 202 1.
REPEAT 215 231 2.
REPEAT 274 290 3; approximate.
DOMAIN 394 576 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
DNA_BIND 423 430
REGION 111 116 Calcineurin-binding.
REGION 119 201 Trans-activation domain A (TAD-A).
REGION 163 177 Required for cytoplasmic retention of the
phosphorylated form.
REGION 186 292 3 X approximate SP repeats.
MOTIF 253 255 Nuclear localization signal.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 53 53 Phosphoserine. {ECO:0000305}.
MOD_RES 54 54 Phosphoserine. {ECO:0000305}.
MOD_RES 56 56 Phosphoserine. {ECO:0000305}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11030334}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000305|PubMed:11030334}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 238 238 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000269|PubMed:11030334}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11030334}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 761 761 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000250|UniProtKB:Q13469}.
VAR_SEQ 619 806 DGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVN
FYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPA
HGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPD
ARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADA
HRSVLVHAGSQGQGQGSTLPHTSS -> GPAGTCETRPLPI
SLISADRLSPWLSRLQRNPPGSVFRCSVLLPAPGSSLVLLA
L (in isoform D).
{ECO:0000303|PubMed:11278367}.
/FTId=VSP_005597.
VAR_SEQ 910 927 VNEIIRKEFSGPPSRNQT -> ELIDTHLSWIQNIL (in
isoform B). {ECO:0000303|PubMed:8668213}.
/FTId=VSP_005596.
MUTAGEN 112 112 R->A: Lowers dephosphorylation.
{ECO:0000269|PubMed:9660947}.
MUTAGEN 114 114 E->A: Lowers dephosphorylation.
{ECO:0000269|PubMed:9660947}.
MUTAGEN 116 116 T->A: No dephosphorylation.
{ECO:0000269|PubMed:9660947}.
MUTAGEN 164 164 R->A: Induces aberrant nuclear
localization of the phosphorylated form.
{ECO:0000269|PubMed:11030334}.
MUTAGEN 423 423 R->A: Decrease in binding to DNA.
{ECO:0000269|PubMed:7876165}.
MUTAGEN 425 425 H->A: No change in binding to DNA.
{ECO:0000269|PubMed:7876165}.
MUTAGEN 426 426 Y->A: Decrease in binding to DNA.
{ECO:0000269|PubMed:7876165}.
MUTAGEN 428 428 T->A: No change in binding to DNA.
{ECO:0000269|PubMed:7876165}.
MUTAGEN 428 428 T->C: No change in binding to DNA and
confers DNA-binding sensitivity to
sulfhydryl modifications.
{ECO:0000269|PubMed:7876165}.
MUTAGEN 429 429 E->A: Decrease in binding to DNA.
{ECO:0000269|PubMed:7876165}.
CONFLICT 78 78 L -> P (in Ref. 3; AAK49895).
{ECO:0000305}.
CONFLICT 287 287 L -> P (in Ref. 2; AAC52929/AAC52930/
AAC52931). {ECO:0000305}.
CONFLICT 802 802 P -> R (in Ref. 2; AAC52929/AAC52930/
AAC52931). {ECO:0000305}.
SEQUENCE 927 AA; 100020 MW; F21E7BABE7DBB40F CRC64;
MDVPEPQPDP DGGDGPGHEP GGSPQDELDF SILFDYDYLN PIEEEPIAHK AISSPSGLAY
PDDVLDYGLK PCNPLASLSG EPPGRFGEPD SIGFQNFLSP VKPAGASGPS PRIEITPSHE
LMQAGGALRG RDAGLSPEQP ALALAGVAAS PRFTLPVPGY EGYREPLCLS PASSGSSASF
ISDTFSPYTS PCVSPNNAGP DDLCPQFQNI PAHYSPRTSP IMSPRTSLAE DSCLGRHSPV
PRPASRSSSP GAKRRHSCAE ALVAPLPAAS PQRSRSPSPQ PSPHVALQDD SIPAGYPPTA
GSAVLMDALN TLATDSPCGI PSKIWKTSPD PTPVSTAPSK AGLARHIYPT VEFLGPCEQE
ERRNSAPESI LLVPPTWPKQ LVPAIPICSI PVTASLPPLE WPLSNQSGSY ELRIEVQPKP
HHRAHYETEG SRGAVKAPTG GHPVVQLHGY MENKPLGLQI FIGTADERIL KPHAFYQVHR
ITGKTVTTTS YEKIVGNTKV LEIPLEPKNN MRATIDCAGI LKLRNADIEL RKGETDIGRK
NTRVRLVFRV HVPEPSGRIV SLQAASNPIE CSQRSAHELP MVERQDMDSC LVYGGQQMIL
TGQNFTAESK VVFMEKTTDG QQIWEMEATV DKDKSQPNML FVEIPEYRNK HIRVPVKVNF
YVINGKRKRS QPQHFTYHPV PAIKTEPSDE YEPSLICSPA HGGLGSQPYY PQHPMLAESP
SCLVATMAPC QQFRSGLSSP DARYQQQSPA AALYQRSKSL SPGLLGYQQP SLLAAPLGLA
DAHRSVLVHA GSQGQGQGST LPHTSSASQQ ASPVIHYSPT NQQLRGGGHQ EFQHIMYCEN
FGPSSARPGP PPINQGQRLS PGAYPTVIQQ QTAPSQRAAK NGPSDQKEAL PTGVTVKQEQ
NLDQTYLDDV NEIIRKEFSG PPSRNQT


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28-985 Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor respons 0.05 mg
28-339 Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of the interleukin 2 gene. NFAT binds to a sequence in the interleukin 2 gene enhancer known as the 0.1 mg
DL-NFATC2-Hu Human Nuclear Factor Of Activated T-Cells,Cytoplasmic 2 (NFATC2) ELISA Kit 96T
EIAAB27032 Bos taurus,Bovine,NFAT transcription complex cytosolic component,NFATc,NF-ATc,NFATc1,NFATC1,NF-ATc1,Nuclear factor of activated T-cells, cytoplasmic 1
18-003-43811 Nuclear factor of activated T-cells. cytoplasmic 4 - NF-ATc4; NFATc4; T-cell transcription factor NFAT3; NF-AT3 Polyclonal 0.05 mg Aff Pur
18-003-43424 Nuclear factor of activated T-cells. cytoplasmic 4 - NF-ATc4; NFATc4; T-cell transcription factor NFAT3; NF-AT3 Polyclonal 0.1 mg Protein A
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27030 Mouse,Mus musculus,NFAT transcription complex cytosolic component,Nfat2,NFATc,Nfatc,NF-ATc,NFATc1,Nfatc1,NF-ATc1,Nuclear factor of activated T-cells, cytoplasmic 1
EIAAB27029 NFAT transcription complex cytosolic component,NFAT2,NFATc,NFATC,NF-ATc,NFATc1,NFATC1,NF-ATc1,NFATmac,Nuclear factor of activated T-cells, cytoplasmic 1,Pig,Sus scrofa
EIAAB27031 Homo sapiens,Human,NFAT transcription complex cytosolic component,NFAT2,NFATc,NFATC,NF-ATc,NFATc1,NFATC1,NF-ATc1,Nuclear factor of activated T-cells, cytoplasmic 1
CSB-EL015746HU Human Nuclear factor of activated T-cells, cytoplasmic 2(NFATC2) ELISA kit 96T
CSB-EL015746MO Mouse Nuclear factor of activated T-cells, cytoplasmic 2(NFATC2) ELISA kit 96T
CSB-EL015746MO Mouse Nuclear factor of activated T-cells, cytoplasmic 2(NFATC2) ELISA kit SpeciesMouse 96T
NFATC3 NFATC2 Gene nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 2
CSB-EL015746HU Human Nuclear factor of activated T-cells, cytoplasmic 2(NFATC2) ELISA kit SpeciesHuman 96T
10-P1664 Polyclonal antibody Anti-Nuclear factor of activated T-cells, cytoplasmic 2, NFATC2 100μg
ARP37106_T200 Anti-Nuclear factor of activated T-cells, cytoplasmic 2 (Nfatc2) Species_Reactivity: Mouse
SEL942Hu ELISA Kit for Nuclear Factor Of Activated T-Cells, Cytoplasmic 2 (NFATC2) Homo sapiens (Human) 96T
NFAC2_MOUSE ELISA Kit FOR Nuclear factor of activated T-cells, cytoplasmic 2; organism: Mouse; gene name: Nfatc2 96T
E80942Hu ELISA Kit for Nuclear Factor Of Activated T-Cells, Cytoplasmic 2 (NFATC2) Organism: Homo sapiens (Human) 96T
EIAAB27037 Mouse,Mus musculus,Nfat3,NF-AT3,NFATc4,Nfatc4,NF-ATc4,Nuclear factor of activated T-cells, cytoplasmic 4,T-cell transcription factor NFAT3
EIAAB27038 Homo sapiens,Human,NFAT3,NF-AT3,NFATc4,NFATC4,NF-ATc4,Nuclear factor of activated T-cells, cytoplasmic 4,T-cell transcription factor NFAT3


 

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