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Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (IL-2-inducible T-cell kinase) (Kinase EMT) (Kinase TLK) (T-cell-specific kinase)

 ITK_MOUSE               Reviewed;         625 AA.
Q03526;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 183.
RecName: Full=Tyrosine-protein kinase ITK/TSK;
EC=2.7.10.2;
AltName: Full=IL-2-inducible T-cell kinase;
AltName: Full=Kinase EMT;
AltName: Full=Kinase TLK;
AltName: Full=T-cell-specific kinase;
Name=Itk; Synonyms=Emt, Tlk, Tsk;
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].
TISSUE=Thymocyte;
PubMed=1280821; DOI=10.1073/pnas.89.23.11194;
Siliciano J.D., Morrow T.A., Desiderio S.V.;
"itk, a T-cell-specific tyrosine kinase gene inducible by interleukin
2.";
Proc. Natl. Acad. Sci. U.S.A. 89:11194-11198(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymocyte;
PubMed=8421704; DOI=10.1073/pnas.90.2.669;
Heyeck S.D., Berg L.J.;
"Developmental regulation of a murine T-cell-specific tyrosine kinase
gene, Tsk.";
Proc. Natl. Acad. Sci. U.S.A. 90:669-673(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CBA/J; TISSUE=Mast cell;
PubMed=8476425; DOI=10.1006/bbrc.1993.1404;
Yamada N., Kawakami Y., Kimura H., Fukamachi H., Baier G., Altman A.,
Kato T., Inagaki Y., Kawakami T.;
"Structure and expression of novel protein-tyrosine kinases, Emb and
Emt, in hematopoietic cells.";
Biochem. Biophys. Res. Commun. 192:231-240(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Ogata M., Sawada M., Fujiwara H., Hamaoka T.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[5]
DISRUPTION PHENOTYPE.
PubMed=8777721; DOI=10.1016/1074-7613(95)90065-9;
Liao X.C., Littman D.R.;
"Altered T cell receptor signaling and disrupted T cell development in
mice lacking Itk.";
Immunity 3:757-769(1995).
[6]
FUNCTION, INTERACTION WITH TBX21, AND SUBCELLULAR LOCATION.
PubMed=15662016; DOI=10.1126/science.1103336;
Hwang E.S., Szabo S.J., Schwartzberg P.L., Glimcher L.H.;
"T helper cell fate specified by kinase-mediated interaction of T-bet
with GATA-3.";
Science 307:430-433(2005).
[7]
INTERACTION WITH THEMIS.
PubMed=19597499; DOI=10.1038/ni.1766;
Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C.,
Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J.,
Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J.;
"Themis controls thymocyte selection through regulation of T cell
antigen receptor-mediated signaling.";
Nat. Immunol. 10:848-856(2009).
[8]
STRUCTURE BY NMR OF 160-236.
PubMed=8985255; DOI=10.1038/385093a0;
Andreotti A.H., Bunnell S.C., Feng S., Berg L.J., Schreiber S.L.;
"Regulatory intramolecular association in a tyrosine kinase of the Tec
family.";
Nature 385:93-97(1997).
[9]
CHARACTERIZATION.
PubMed=7524075; DOI=10.1073/pnas.91.20.9347;
August A., Gibson S., Kawakami Y., Kawakami T., Mills G.B., Dupont B.;
"CD28 is associated with and induces the immediate tyrosine
phosphorylation and activation of the Tec family kinase ITK/EMT in the
human Jurkat leukemic T-cell line.";
Proc. Natl. Acad. Sci. U.S.A. 91:9347-9351(1994).
[10]
CHARACTERIZATION.
PubMed=8943565; DOI=10.1093/intimm/8.11.1707;
King P.D., Sadra A., Han A., Liu X.-R., Sunder-Plassmann R.,
Reinherz E.L., Dupont B.;
"CD2 signaling in T cells involves tyrosine phosphorylation and
activation of the Tec family kinase, EMT/ITK/TSK.";
Int. Immunol. 8:1707-1714(1996).
[11]
CHARACTERIZATION.
PubMed=10570288;
Ching K.A., Kawakami Y., Kawakami T., Tsoukas C.D.;
"Emt/Itk associates with activated TCR complexes: role of the
pleckstrin homology domain.";
J. Immunol. 163:6006-6013(1999).
[12]
DISRUPTION PHENOTYPE.
PubMed=10213685; DOI=10.1126/science.284.5414.638;
Schaeffer E.M., Debnath J., Yap G., McVicar D., Liao X.C.,
Littman D.R., Sher A., Varmus H.E., Lenardo M.J., Schwartzberg P.L.;
"Requirement for Tec kinases Rlk and Itk in T cell receptor signaling
and immunity.";
Science 284:638-641(1999).
[13]
DISRUPTION PHENOTYPE.
PubMed=16860760; DOI=10.1016/j.immuni.2006.05.011;
Broussard C., Fleischacker C., Horai R., Chetana M., Venegas A.M.,
Sharp L.L., Hedrick S.M., Fowlkes B.J., Schwartzberg P.L.;
"Altered development of CD8+ T cell lineages in mice deficient for the
Tec kinases Itk and Rlk.";
Immunity 25:93-104(2006).
[14]
SUBUNIT.
PubMed=20237289; DOI=10.4049/jimmunol.0901908;
Min L., Wu W., Joseph R.E., Fulton D.B., Berg L., Andreotti A.H.;
"Disrupting the intermolecular self-association of Itk enhances T cell
signaling.";
J. Immunol. 184:4228-4235(2010).
[15]
FUNCTION IN INVARIANT NKT CELL MATURATION, AND DISRUPTION PHENOTYPE.
PubMed=21036902; DOI=10.1074/jbc.M110.148205;
Qi Q., Xia M., Bai Y., Yu S., Cantorna M., August A.;
"Interleukin-2-inducible T cell kinase (Itk) network edge dependence
for the maturation of iNKT cell.";
J. Biol. Chem. 286:138-146(2011).
-!- FUNCTION: Tyrosine kinase that plays an essential role in
regulation of the adaptive immune response. Regulates the
development, function and differentiation of conventional T-cells
and nonconventional NKT-cells. When antigen presenting cells (APC)
activate T-cell receptor (TCR), a series of phosphorylation lead
to the recruitment of ITK to the cell membrane, in the vicinity of
the stimulated TCR receptor, where it is phosphorylated by LCK.
Phosphorylation leads to ITK autophosphorylation and full
activation. Once activated, phosphorylates PLCG1, leading to the
activation of this lipase and subsequent cleavage of its
substrates. In turn, the endoplasmic reticulum releases calcium in
the cytoplasm and the nuclear activator of activated T-cells
(NFAT) translocates into the nucleus to perform its
transcriptional duty. Phosphorylates 2 essential adapter proteins:
the linker for activation of T-cells/LAT protein and LCP2. Then, a
large number of signaling molecules such as VAV1 are recruited and
ultimately lead to lymphokine production, T-cell proliferation and
differentiation. Phosphorylates TBX21 at 'Tyr-525' and mediates
its interaction with GATA3 (PubMed:15662016).
{ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21036902}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homooligomerizes; this association negatively regulates
kinase activity. Interacts with PPIA/CYPA; this interaction
regulates TCR signal strength via a proline-directed
conformational switch in ITK. Interacts with THEMIS (By
similarity). Interacts with FASLG. Interacts with VAV1; this
interaction is important for VAV1 localization and TCR-induced
actin polarization. Interacts with TBX21 (PubMed:15662016).
{ECO:0000250|UniProtKB:Q08881, ECO:0000269|PubMed:15662016,
ECO:0000269|PubMed:19597499, ECO:0000269|PubMed:20237289}.
-!- INTERACTION:
P08487:PLCG1 (xeno); NbExp=4; IntAct=EBI-647969, EBI-8013886;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
{ECO:0000269|PubMed:15662016}. Note=Localizes in the vicinity of
cell surface receptors in the plasma membrane after receptor
stimulation. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Is detected in the thymus, lymph node and very
faintly in the spleen, but is not detected in the liver, lung,
kidney, heart, brain, intestine or testis. Expressed in T-
lymphocytes and mast cells. It may also be expressed in natural
killer cells.
-!- DEVELOPMENTAL STAGE: Is present in the fetal thymus as early as
day 14 of gestation. The levels are 5- to 10-fold higher in
thymocytes than in peripheral T-cells, and increase in the thymus
during development from neonate to adult.
-!- INDUCTION: Through a myriad of surface receptors including the
TCR/CD3 signaling complex, coreceptors, or chemokine receptors.
-!- DOMAIN: The N-terminal PH domain allows ITK to be recruited to the
plasma membrane by an activated PI3 kinase. This domain contains
also a proline-rich region (PRR). The adjoining domain is a SH3
domain, which binds to PRR (from itself or from other proteins).
Next, a SH2 domain is required for binding tyrosine-phosphorylated
substrates. In the C-terminal region, the kinase domain is
required for tyrosine phosphorylation (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated at Tyr-517 in the activation loop of the
kinase domain by LCK. Subsequent autophosphorylation at Tyr-186
leads to the kinase activation. The autophosphorylated Tyr-186
lies within the substrate binding sequence of the SH3 domain (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display decreased mature thymocytes and
elicit profound defect in CD4+ and CD8+ T-cell development.
Additionally, they show a strong decrease of cytokine production
in response to TCR receptor stimulation.
{ECO:0000269|PubMed:10213685, ECO:0000269|PubMed:16860760,
ECO:0000269|PubMed:21036902, ECO:0000269|PubMed:8777721}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. TEC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; L00619; AAA39337.1; -; mRNA.
EMBL; L05631; AAA40518.1; -; mRNA.
EMBL; L10628; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; D14042; BAA03129.1; -; mRNA.
CCDS; CCDS70169.1; -.
PIR; A43030; A43030.
RefSeq; NP_001268894.1; NM_001281965.1.
RefSeq; NP_001268895.1; NM_001281966.1.
RefSeq; NP_001268897.1; NM_001281968.1.
RefSeq; NP_034713.2; NM_010583.3.
UniGene; Mm.339927; -.
PDB; 1AWJ; NMR; -; A=160-236.
PDB; 1LUI; NMR; -; A=238-344.
PDB; 1LUK; NMR; -; A=238-344.
PDB; 1LUM; NMR; -; A=238-344.
PDB; 1LUN; NMR; -; A=238-344.
PDB; 2ETZ; NMR; -; A=238-344.
PDB; 2EU0; NMR; -; A=238-344.
PDB; 2K79; NMR; -; A=177-237, B=238-344.
PDB; 2K7A; NMR; -; A=177-237, B=238-344.
PDB; 2RN8; NMR; -; A=177-238.
PDB; 2RNA; NMR; -; A=177-238.
PDB; 3S9K; X-ray; 2.35 A; A=236-344.
PDBsum; 1AWJ; -.
PDBsum; 1LUI; -.
PDBsum; 1LUK; -.
PDBsum; 1LUM; -.
PDBsum; 1LUN; -.
PDBsum; 2ETZ; -.
PDBsum; 2EU0; -.
PDBsum; 2K79; -.
PDBsum; 2K7A; -.
PDBsum; 2RN8; -.
PDBsum; 2RNA; -.
PDBsum; 3S9K; -.
ProteinModelPortal; Q03526; -.
SMR; Q03526; -.
BioGrid; 200840; 5.
DIP; DIP-29283N; -.
IntAct; Q03526; 7.
MINT; MINT-84965; -.
STRING; 10090.ENSMUSP00000020664; -.
iPTMnet; Q03526; -.
PhosphoSitePlus; Q03526; -.
EPD; Q03526; -.
MaxQB; Q03526; -.
PaxDb; Q03526; -.
PRIDE; Q03526; -.
Ensembl; ENSMUST00000109237; ENSMUSP00000104860; ENSMUSG00000020395.
GeneID; 16428; -.
KEGG; mmu:16428; -.
UCSC; uc011xtn.2; mouse.
CTD; 3702; -.
MGI; MGI:96621; Itk.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233859; -.
HOVERGEN; HBG008761; -.
InParanoid; Q03526; -.
KO; K07363; -.
OMA; RYPVCSW; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; Q03526; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.1; 3474.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
EvolutionaryTrace; Q03526; -.
PRO; PR:Q03526; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020395; -.
CleanEx; MM_ITK; -.
ExpressionAtlas; Q03526; baseline and differential.
Genevisible; Q03526; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; IMP:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
GO; GO:0001816; P:cytokine production; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0032609; P:interferon-gamma production; IMP:MGI.
GO; GO:0032633; P:interleukin-4 production; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0001865; P:NK T cell differentiation; IMP:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd11908; SH3_ITK; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035583; ITK_SH3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001562; Znf_Btk_motif.
Pfam; PF00779; BTK; 1.
Pfam; PF00169; PH; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00402; TECBTKDOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00107; BTK; 1.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS51113; ZF_BTK; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; ATP-binding; Complete proteome;
Cytoplasm; Immunity; Kinase; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 625 Tyrosine-protein kinase ITK/TSK.
/FTId=PRO_0000088107.
DOMAIN 4 117 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 177 237 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 245 343 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 368 620 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 119 155 Btk-type. {ECO:0000255|PROSITE-
ProRule:PRU00432}.
NP_BIND 374 382 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 487 487 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 127 127 Zinc. {ECO:0000250}.
METAL 138 138 Zinc. {ECO:0000250}.
METAL 139 139 Zinc. {ECO:0000250}.
METAL 149 149 Zinc. {ECO:0000250}.
BINDING 396 396 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 186 186 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q08881}.
MOD_RES 517 517 Phosphotyrosine; by LCK.
{ECO:0000250|UniProtKB:Q08881}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:Q08881}.
CONFLICT 82 87 Missing (in Ref. 2, 3 and 4).
{ECO:0000305}.
CONFLICT 535 535 F -> S (in Ref. 3; L10628).
{ECO:0000305}.
CONFLICT 540 540 Y -> C (in Ref. 3; L10628).
{ECO:0000305}.
STRAND 178 180 {ECO:0000244|PDB:1AWJ}.
STRAND 181 186 {ECO:0000244|PDB:2K79}.
STRAND 192 195 {ECO:0000244|PDB:2K79}.
STRAND 200 202 {ECO:0000244|PDB:1AWJ}.
STRAND 203 205 {ECO:0000244|PDB:2K79}.
STRAND 211 214 {ECO:0000244|PDB:1AWJ}.
STRAND 215 218 {ECO:0000244|PDB:2RN8}.
STRAND 220 222 {ECO:0000244|PDB:1AWJ}.
STRAND 224 226 {ECO:0000244|PDB:2K79}.
STRAND 229 234 {ECO:0000244|PDB:2K79}.
HELIX 240 242 {ECO:0000244|PDB:3S9K}.
STRAND 243 246 {ECO:0000244|PDB:2ETZ}.
STRAND 248 250 {ECO:0000244|PDB:2K79}.
HELIX 252 262 {ECO:0000244|PDB:3S9K}.
STRAND 268 272 {ECO:0000244|PDB:3S9K}.
TURN 275 277 {ECO:0000244|PDB:1LUI}.
STRAND 279 285 {ECO:0000244|PDB:3S9K}.
STRAND 290 292 {ECO:0000244|PDB:3S9K}.
STRAND 294 302 {ECO:0000244|PDB:3S9K}.
STRAND 305 307 {ECO:0000244|PDB:1LUM}.
STRAND 310 313 {ECO:0000244|PDB:3S9K}.
STRAND 318 320 {ECO:0000244|PDB:1LUI}.
HELIX 321 330 {ECO:0000244|PDB:3S9K}.
STRAND 335 337 {ECO:0000244|PDB:3S9K}.
STRAND 338 342 {ECO:0000244|PDB:1LUK}.
SEQUENCE 625 AA; 72292 MW; F7A4A18A8A1AADDC CRC64;
MNNFILLEEQ LIKKSQQKRR TSPSNFKVRF FVLTKASLAY FEDRHGKKRT LKGSIELSRI
KCVEIVKSDI SIPCHYKYPF QTLVYLQVVH DNYLLYVFAP DCESRQRWVL TLKEETRNNN
SLVSKYHPNF WMDGRWRCCS QLEKPAVGCA PYDPSKNASK KPLPPTPEDN RRSFQEPEET
LVIALYDYQT NDPQELALRC DEEYYLLDSS EIHWWRVQDK NGHEGYAPSS YLVEKSPNNL
ETYEWYNKSI SRDKAEKLLL DTGKEGAFMV RDSRTPGTYT VSVFTKAIIS ENPCIKHYHI
KETNDSPKRY YVAEKYVFDS IPLLIQYHQY NGGGLVTRLR YPVCSWRQKA PVTAGLRYGK
WVIQPSELTF VQEIGSGQFG LVHLGYWLNK DKVAIKTIQE GAMSEEDFIE EAEVMMKLSH
PKLVQLYGVC LEQAPICLVF EFMEHGCLSD YLRSQRGLFA AETLLGMCLD VCEGMAYLEK
ACVIHRDLAA RNCLVGENQV IKVSDFGMTR FVLDDQYTSS TGTKFPVKWA SPEVFSFSRY
SSKSDVWSFG VLMWEVFSEG KIPYENRSNS EVVEDISTGF RLYKPRLASC HVYQIMNHCW
KEKPEDRPPF SQLLSQLAEI AEAGL


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EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
18-661-15209 Tyrosine-protein kinase BTK - EC 2.7.10.2; Bruton tyrosine kinase; Agammaglobulinaemia tyrosine kinase; ATK; B cell progenitor kinase; BPK Polyclonal 0.1 mg
EIAAB14369 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,Fak2,Focal adhesion kinase 2,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,Ptk2b,Pyk2,Rat,Rattus norve
EIAAB14370 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,FAK2,Focal adhesion kinase 2,Homo sapiens,Human,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,PTK2B,PY
EIAAB14368 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,Fak2,Focal adhesion kinase 2,Mouse,Mus musculus,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,Ptk2b,Py
18-003-42265 Protein tyrosine kinase 2 beta - EC 2.7.10.2; Focal adhesion kinase 2; FADK 2; Proline-rich tyrosine kinase 2; Cell adhesion kinase beta; CAK beta; Calcium-dependent tyrosine kinase; CADTK; Related ad 0.1 mg Protein A
18-003-42266 Protein tyrosine kinase 2 beta - EC 2.7.10.2; Focal adhesion kinase 2; FADK 2; Proline-rich tyrosine kinase 2; Cell adhesion kinase beta; CAK beta; Calcium-dependent tyrosine kinase; CADTK; Related ad 0.05 mg Aff Pur
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
E0039h ELISA kit CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,ST 96T
U0039h CLIA CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,STK1,STK 96T
E0039h ELISA CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,STK1,ST 96T
10-782-55045 Proto-oncogene tyrosine-protein kinase LCK - EC 2.7.10.2; p56-LCK; Lymphocyte cell-specific protein-tyrosine kinase; LSK; T cell-specific protein-tyrosine kinase N_A 0.005 mg


 

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