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B-cell lymphoma/leukemia 11B (BCL-11B) (B-cell CLL/lymphoma 11B) (COUP-TF-interacting protein 2) (Radiation-induced tumor suppressor gene 1 protein) (mRit1)

 BC11B_MOUSE             Reviewed;         884 AA.
Q99PV8; Q8C2I1; Q99PV6; Q99PV7; Q9JLF8;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
31-JAN-2018, entry version 140.
RecName: Full=B-cell lymphoma/leukemia 11B;
Short=BCL-11B;
AltName: Full=B-cell CLL/lymphoma 11B;
AltName: Full=COUP-TF-interacting protein 2;
AltName: Full=Radiation-induced tumor suppressor gene 1 protein;
Short=mRit1;
Name=Bcl11b; Synonyms=Ctip2, Rit1;
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] (ISOFORMS 1; 2 AND 3), AND VARIANTS
THR-676; CYS-783 AND SER-849.
PubMed=12565905; DOI=10.1016/S0006-291X(02)03069-3;
Wakabayashi Y., Inoue J., Takahashi Y., Matsuki A., Kosugi-Okano H.,
Shinbo T., Mishima Y., Niwa O., Kominami R.;
"Homozygous deletions and point mutations of the Rit1/Bcl11b gene in
gamma-ray induced mouse thymic lymphomas.";
Biochem. Biophys. Res. Commun. 301:598-603(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH TFCOUP1;
EAR2 AND ARP1.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10744719; DOI=10.1074/jbc.275.14.10315;
Avram D., Fields A., Pretty On Top K., Nevrivy D.J., Ishmael J.E.,
Leid M.;
"Isolation of a novel family of C(2)H(2) zinc finger proteins
implicated in transcriptional repression mediated by chicken ovalbumin
upstream promoter transcription factor (COUP-TF) orphan nuclear
receptors.";
J. Biol. Chem. 275:10315-10322(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-884.
STRAIN=NOD; TISSUE=Thymus;
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).
[5]
FUNCTION.
PubMed=12717433; DOI=10.1038/ni927;
Wakabayashi Y., Watanabe H., Inoue J., Takeda N., Sakata J.,
Mishima Y., Hitomi J., Yamamoto T., Utsuyama M., Niwa O., Aizawa S.,
Kominami R.;
"Bcl11b is required for differentiation and survival of alphabeta T
lymphocytes.";
Nat. Immunol. 4:533-539(2003).
[6]
INTERACTION WITH SIRT1.
PubMed=12930829; DOI=10.1074/jbc.M307477200;
Senawong T., Peterson V.J., Avram D., Shepherd D.M., Frye R.A.,
Minucci S., Leid M.;
"Involvement of the histone deacetylase SIRT1 in chicken ovalbumin
upstream promoter transcription factor (COUP-TF)-interacting protein
2-mediated transcriptional repression.";
J. Biol. Chem. 278:43041-43050(2003).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16809611; DOI=10.1182/blood-2006-05-021790;
Cismasiu V.B., Ghanta S., Duque J., Albu D.I., Chen H.M., Kasturi R.,
Avram D.;
"BCL11B participates in the activation of IL2 gene expression in CD4+
T lymphocytes.";
Blood 108:2695-2702(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-109; SER-128;
THR-260; THR-376; SER-381; SER-401; THR-406; THR-416; SER-495;
SER-496; THR-744 AND SER-762, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, 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).
[9]
SUMOYLATION WITH SUMO1.
PubMed=23213215; DOI=10.1073/pnas.1215366110;
Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
"In vivo localization and identification of SUMOylated proteins in the
brain of His6-HA-SUMO1 knock-in mice.";
Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-293 AND ARG-322, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Key regulator of both differentiation and survival of T-
lymphocytes during thymocyte development in mammals
(PubMed:12717433). Essential in controlling the responsiveness of
hematopoietic stem cells to chemotactic signals by modulating the
expression of receptors CCR7 and CCR9, which direct the movement
of progenitor cells from the bone marrow to the thymus (By
similarity). Is a regulator of IL2 promoter and enhances IL2
expression in activated CD4(+) T-lymphocytes (PubMed:16809611).
Tumor-suppressor protein involved in T-cell lymphomas. May
function on the P53-signaling pathway. Repress transcription
through direct, TFCOUP2-independent binding to a GC-rich response
element. {ECO:0000250|UniProtKB:Q9C0K0,
ECO:0000269|PubMed:12717433, ECO:0000269|PubMed:16809611}.
-!- SUBUNIT: Interacts with TFCOUP1, SIRT1, ARP1 and EAR2
(PubMed:10744719, PubMed:12930829). Interacts with EP300; the
interaction is detected in activated T-lymphocytes, but not under
resting conditions (By similarity). {ECO:0000250|UniProtKB:Q9C0K0,
ECO:0000269|PubMed:10744719, ECO:0000269|PubMed:12930829}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=Q99PV8-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q99PV8-2; Sequence=VSP_009568;
Note=May be due to exon skipping.;
Name=3; Synonyms=Gamma;
IsoId=Q99PV8-3; Sequence=VSP_009566;
Note=May be due to exon skipping.;
-!- TISSUE SPECIFICITY: Expressed in brain and thymus. Expressed in
splenic CD4(+) T-lymphocytes (PubMed:16809611).
{ECO:0000269|PubMed:16809611}.
-!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
-!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
-!- SEQUENCE CAUTION:
Sequence=AAF63683.1; Type=Frameshift; Positions=135, 221, 227, 252, 259, 264; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB043551; BAB32728.1; -; mRNA.
EMBL; AB043553; BAB32729.1; -; mRNA.
EMBL; AB043583; BAB32730.1; -; mRNA.
EMBL; AF186019; AAF63683.1; ALT_FRAME; mRNA.
EMBL; BC019503; AAH19503.1; -; mRNA.
EMBL; AK088588; BAC40438.1; -; mRNA.
CCDS; CCDS36552.1; -. [Q99PV8-2]
CCDS; CCDS36553.1; -. [Q99PV8-1]
CCDS; CCDS70419.1; -. [Q99PV8-3]
RefSeq; NP_001073352.1; NM_001079883.1. [Q99PV8-1]
RefSeq; NP_001273272.1; NM_001286343.1.
RefSeq; NP_067374.2; NM_021399.2. [Q99PV8-2]
UniGene; Mm.392694; -.
ProteinModelPortal; Q99PV8; -.
SMR; Q99PV8; -.
BioGrid; 208391; 5.
IntAct; Q99PV8; 1.
STRING; 10090.ENSMUSP00000068258; -.
iPTMnet; Q99PV8; -.
PhosphoSitePlus; Q99PV8; -.
PaxDb; Q99PV8; -.
PeptideAtlas; Q99PV8; -.
PRIDE; Q99PV8; -.
Ensembl; ENSMUST00000066060; ENSMUSP00000068258; ENSMUSG00000048251. [Q99PV8-1]
Ensembl; ENSMUST00000109891; ENSMUSP00000105517; ENSMUSG00000048251. [Q99PV8-2]
GeneID; 58208; -.
KEGG; mmu:58208; -.
UCSC; uc007ozh.1; mouse. [Q99PV8-1]
UCSC; uc007ozi.1; mouse. [Q99PV8-2]
CTD; 64919; -.
MGI; MGI:1929913; Bcl11b.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063542; -.
HOGENOM; HOG000015256; -.
HOVERGEN; HBG050673; -.
InParanoid; Q99PV8; -.
KO; K22046; -.
OMA; DDAGGCG; -.
OrthoDB; EOG091G160N; -.
PhylomeDB; Q99PV8; -.
TreeFam; TF318131; -.
PRO; PR:Q99PV8; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000048251; -.
CleanEx; MM_BCL11B; -.
CleanEx; MM_RIT1; -.
ExpressionAtlas; Q99PV8; baseline and differential.
Genevisible; Q99PV8; MM.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0021953; P:central nervous system neuron differentiation; IGI:MGI.
GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IGI:MGI.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
GO; GO:0035701; P:hematopoietic stem cell migration; ISS:UniProtKB.
GO; GO:0003334; P:keratinocyte development; IMP:MGI.
GO; GO:0097535; P:lymphoid lineage cell migration into thymus; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0071678; P:olfactory bulb axon guidance; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0043368; P:positive T cell selection; IMP:MGI.
GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:MGI.
GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0021773; P:striatal medium spiny neuron differentiation; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0033153; P:T cell receptor V(D)J recombination; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
Gene3D; 4.10.1050.10; -; 1.
InterPro; IPR026939; At2g23090-like.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 6.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 884 B-cell lymphoma/leukemia 11B.
/FTId=PRO_0000047105.
ZN_FING 221 251 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 426 453 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 454 481 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 786 813 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 814 843 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 844 874 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 560 647 Gly-rich.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 119 119 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 260 260 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 293 293 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 322 322 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 376 376 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 406 406 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 416 416 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 744 744 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C0K0}.
MOD_RES 762 762 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 841 841 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9C0K0}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9C0K0}.
CROSSLNK 587 587 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9C0K0}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9C0K0}.
CROSSLNK 713 713 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9C0K0}.
CROSSLNK 877 877 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9C0K0}.
VAR_SEQ 21 214 Missing (in isoform 3).
{ECO:0000303|PubMed:12565905}.
/FTId=VSP_009566.
VAR_SEQ 142 213 Missing (in isoform 2).
{ECO:0000303|PubMed:10744719,
ECO:0000303|PubMed:12565905,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_009568.
VARIANT 676 676 K -> T (in gamma induced thymic
lymphomas).
{ECO:0000269|PubMed:12565905}.
VARIANT 783 783 R -> C (in gamma induced thymic
lymphomas).
{ECO:0000269|PubMed:12565905}.
VARIANT 849 849 C -> S (in gamma induced thymic
lymphomas).
{ECO:0000269|PubMed:12565905}.
CONFLICT 20 20 P -> R (in Ref. 1; BAB32730).
{ECO:0000305}.
CONFLICT 379 379 P -> S (in Ref. 2; AAF63683).
{ECO:0000305}.
CONFLICT 806 807 RS -> KN (in Ref. 2; AAF63683).
{ECO:0000305}.
SEQUENCE 884 AA; 94566 MW; 9A86B7E34450B2F2 CRC64;
MSRRKQGNPQ HLSQRELITP EADHVEATIL EEDEGLEIEE PSSLGLMVGG PDPDLLTCGQ
CQMNFPLGDI LVFIEHKKKQ CGGLGPCYDK VLDKSSPPPS SRSELRRVSE PVEIGIQVTP
DEDDHLLSPT KGICPKQENI AGPCRPAQLP SMAPIAASSS HPPTSVITSP LRALGVLPPC
FPLPCCGARP ISGDGTQGEG QMEAPFGCQC ELSGKDEPSS YICTTCKQPF NSAWFLLQHA
QNTHGFRIYL EPGPASTSLT PRLTIPPPLG PETVAQSPLM NFLGDSNPFN LLRMTGPILR
DHPGFGEGRL PGTPPLFSPP PRHHLDPHRL SAEEMGLVAQ HPSAFDRVMR LNPMAIDSPA
MDFSRRLREL AGNSSTPPPV SPGRGNPMHR LLNPFQPSPK SPFLSTPPLP PMPAGTPPPQ
PPAKSKSCEF CGKTFKFQSN LIVHRRSHTG EKPYKCQLCD HACSQASKLK RHMKTHMHKA
GSLAGRSDDG LSAASSPEPG TSELPGDLKA ADGDFRHHES DPSLGPEPED DEDEEEEEEE
LLLENESRPE SSFSMDSELG RGRENGGGVP PGVAGAGAAA AALADEKALA LGKVMEDAGL
GALPQYGEKR GAFLKRAGDT GDAGAVGCGD AGAPGAVNGR GGAFAPGAEP FPALFPRKPA
PLPSPGLGGP ALHAAKRIKV EKDLELPPAA LIPSENVYSQ WLVGYAASRH FMKDPFLGFT
DARQSPFATS SEHSSENGSL RFSTPPGDLL DGGLSGRSGT ASGGSTPHLG GPGPGRPSSK
EGRRSDTCEY CGKVFKNCSN LTVHRRSHTG ERPYKCELCN YACAQSSKLT RHMKTHGQIG
KEVYRCDICQ MPFSVYSTLE KHMKKWHGEH LLTNDVKIEQ AERS


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LYS063 HUMAN LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, Isotypes , Applications WB, 0.1 mg
SCH-LYS063A HUMAN LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, Isotypes , Applications WB, 0.5 mg
LYS063B HUMAN LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, Isotypes , Applications WB, 1 mg
LYS063A HUMAN LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, Isotypes , Applications WB, 0.5 mg
SCH-LYS063B HUMAN LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, Isotypes , Applications WB, 1 mg
E1138m Human ELISA Kit FOR T-cell leukemia per lymphoma protein 1B 96T
'CS20-00-002 Human Lymphoma tissue array (Diffuse large cell B-cell T-cell Hodgkin lymphoma follicular diffuse B-cell, etc.) tissues 7 x 9
H4296 T-cell leukemia lymphoma protein 1B (TCL1B), Human, ELISA Kit 96T
UT-E04512 Human T-Cell Leukemia Lymphoma Protein 1A (TCL1A) ELISA Kit 96T
H4295 T-cell leukemia lymphoma protein 1A (TCL1A), Mouse, ELISA Kit 96T
H4294 T-cell leukemia lymphoma protein 1A (TCL1A), Human, ELISA Kit 96T
UB-E04512 Human T-Cell Leukemia per Lymphoma Protein 1A(TCL1A)ELISA Kit 96T
LYS064 HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 0.1 mg
SCH-LYS064B HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 1 mg
LYS064B HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 1 mg
SCH-LYS064A HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 0.5 mg
SCH-LYS064 HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 0.1 mg
LYS064A HUMAN NON_HODGKIN'S LYMPHOMA TUMOR TOTAL PROTEIN LYSATE , Product Type Cell Lysate, Specificity NON_HODGKIN'S LYMPHOMA TUMOR LYSATE, Target Species Human, Host N_A, Format Total Protein Lysate, I 0.5 mg


 

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