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Bcl-2-like protein 11 (Bcl2-L-11) (Bcl2-interacting mediator of cell death)

 B2L11_HUMAN             Reviewed;         198 AA.
O43521; A8K2W2; O43522; Q0MSE7; Q0MSE8; Q0MSE9; Q53R28; Q6JTU6;
Q6T851; Q6TE14; Q6TE15; Q6TE16; Q6V402; Q8WYL6; Q8WYL7; Q8WYL8;
Q8WYL9; Q8WYM0; Q8WYM1;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
27-SEP-2017, entry version 170.
RecName: Full=Bcl-2-like protein 11;
Short=Bcl2-L-11;
AltName: Full=Bcl2-interacting mediator of cell death;
Name=BCL2L11; Synonyms=BIM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL AND BIML), AND FUNCTION.
TISSUE=Peripheral blood, and Spleen;
PubMed=9430630; DOI=10.1093/emboj/17.2.384;
O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M.,
Cory S., Huang D.C.S.;
"Bim: a novel member of the Bcl-2 family that promotes apoptosis.";
EMBO J. 17:384-395(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA1; BIM-ALPHA2;
BIM-BETA1; BIM-BETA2; BIM-BETA3 AND BIM-BETA4), FUNCTION (ISOFORMS
BIM-ALPHA1 AND BIM-ALPHA2), AND SUBCELLULAR LOCATION.
PubMed=11734221; DOI=10.1016/S0014-5793(01)03145-3;
Mami U., Miyashita T., Shikama Y., Tadokoro K., Yamada M.;
"Molecular cloning and characterization of six novel isoforms of human
Bim, a member of the proapoptotic Bcl-2 family.";
FEBS Lett. 509:135-141(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIM-GAMMA), FUNCTION (ISOFORM
BIM-GAMMA), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12019181;
Liu J.-W., Chandra D., Tang S.H., Chopra D., Tang D.G.;
"Identification and characterization of Bimgamma, a novel proapoptotic
BH3-only splice variant of Bim.";
Cancer Res. 62:2976-2981(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMEL; BIML; BIMS; BIM-ALPHA1;
BIM-ALPHA2; BIM-ALPHA3; BIMA; BIMABC AND BIMAC), ALTERNATIVE SPLICING,
FUNCTION, INTERACTION WITH BCL2; BCL2L1 ISOFORM BCL-XL AND BAX, AND
MUTAGENESIS OF GLY-156 AND ASN-160.
TISSUE=Embryonic kidney, and Ovarian cancer;
PubMed=11997495; DOI=10.1128/MCB.22.11.3577-3589.2002;
Marani M., Tenev T., Hancock D., Downward J., Lemoine N.R.;
"Identification of novel isoforms of the BH3 domain protein Bim which
directly activate Bax to trigger apoptosis.";
Mol. Cell. Biol. 22:3577-3589(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIMS AND BIM-ALPHA3), AND
FUNCTION (ISOFORM BIM-ALPHA3).
PubMed=15147734; DOI=10.1016/j.biocel.2003.12.015;
Chen J.Z., Ji C.N., Gu S.H., Li J.X., Zhao E.P., Huang Y., Huang L.,
Ying K., Xie Y., Mao Y.M.;
"Over-expression of Bim alpha3, a novel isoform of human Bim, result
in cell apoptosis.";
Int. J. Biochem. Cell Biol. 36:1554-1561(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BIM-ALPHA3; BIM-ALPHA4;
BIM-ALPHA5; BIM-ALPHA6; BIM-BETA5; BIM-BETA6; BIM-BETA7).
PubMed=17503221; DOI=10.1007/s10495-007-0093-5;
Miao J., Chen G.G., Yun J.P., Chun S.Y., Zheng Z.Z., Ho R.L.K.,
Chak E.C., Xia N.S., Lai P.B.;
"Identification and characterization of BH3 domain protein Bim and its
isoforms in human hepatocellular carcinomas.";
Apoptosis 12:1691-1701(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BIMEL AND BIML).
TISSUE=Teratocarcinoma, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BIMEL).
TISSUE=Blood;
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).
[11]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-69, AND
UBIQUITINATION.
PubMed=15486195;
Fukazawa H., Noguchi K., Masumi A., Murakami Y., Uehara Y.;
"BimEL is an important determinant for induction of anoikis
sensitivity by mitogen-activated protein/extracellular signal-
regulated kinase kinase inhibitors.";
Mol. Cancer Ther. 3:1281-1288(2004).
[12]
MUTAGENESIS OF GLY-156.
PubMed=17289999; DOI=10.1126/science.1133289;
Willis S.N., Fletcher J.I., Kaufmann T., van Delft M.F., Chen L.,
Czabotar P.E., Ierino H., Lee E.F., Fairlie W.D., Bouillet P.,
Strasser A., Kluck R.M., Adams J.M., Huang D.C.;
"Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs,
not Bax or Bak.";
Science 315:856-859(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
INTERACTION WITH TRIM2.
PubMed=21478148; DOI=10.1074/jbc.M110.197707;
Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M.,
Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.;
"Identification of a novel Bcl-2-interacting mediator of cell death
(Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and
its role in rapid ischemic tolerance-induced neuroprotection.";
J. Biol. Chem. 286:19331-19339(2011).
[15]
INDUCTION BY ER STRESS.
PubMed=22761832; DOI=10.1371/journal.pone.0039586;
Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.;
"CHOP potentially co-operates with FOXO3a in neuronal cells to
regulate PUMA and BIM expression in response to ER stress.";
PLoS ONE 7:E39586-E39586(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
INTERACTION WITH BCL2L1; MCL1 AND USP27X.
PubMed=27013495; DOI=10.15252/embr.201541392;
Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
"The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and
enhances apoptosis.";
EMBO Rep. 17:724-738(2016).
[18]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 141-166 IN COMPLEX WITH
MCL1.
PubMed=17389404; DOI=10.1073/pnas.0701297104;
Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J.,
Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.;
"Structural insights into the degradation of Mcl-1 induced by BH3
domains.";
Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 141-165 IN COMPLEX WITH
BCL2A1.
PubMed=18812174; DOI=10.1016/j.febslet.2008.09.028;
Herman M.D., Nyman T., Welin M., Lehtio L., Flodin S., Tresaugues L.,
Kotenyova T., Flores A., Nordlund P.;
"Completing the family portrait of the anti-apoptotic Bcl-2 proteins:
crystal structure of human Bfl-1 in complex with Bim.";
FEBS Lett. 582:3590-3594(2008).
-!- FUNCTION: Induces apoptosis and anoikis. Isoform BimL is more
potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2
and isoform Bim-alpha3 induce apoptosis, although less potent than
isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma
induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly
through a caspase-mediated pathway. Isoform BimAC and isoform
BimABC lack the ability to induce apoptosis.
{ECO:0000269|PubMed:11997495, ECO:0000269|PubMed:15486195,
ECO:0000269|PubMed:9430630}.
-!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L),
BCL2A1/BFL-1, BHRF1, and BCL2L2/BCLW (PubMed:11997495,
PubMed:27013495, PubMed:18812174). Isoform BimS and isoform Bim-
alpha3 interact with BAX; this interaction may lead to BAX
activation through conformational change (PubMed:11997495). Does
not heterodimerize with proapoptotic proteins such as BAD, BOK or
BAK. Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1
isoform Bcl-X(L); BH3 integrity is required for BCL2L1-binding.
Interacts with YWHAZ. When phosphorylated, interacts with TRIM2;
this interaction is associated with ubiquitination and degradation
(PubMed:21478148). Interacts with MCL1; may sequester BCL2L11 to
prevent its pro-apoptotic activity (PubMed:27013495,
PubMed:17389404). When phosphorylated, isoform BimEL interacts
with USP27X; this interaction leads to BCL2L11 deubiquitination
and stabilization (PubMed:27013495). {ECO:0000269|PubMed:11997495,
ECO:0000269|PubMed:17389404, ECO:0000269|PubMed:18812174,
ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.
-!- INTERACTION:
Q92934:BAD; NbExp=2; IntAct=EBI-526406, EBI-700771;
Q07812:BAX; NbExp=20; IntAct=EBI-526406, EBI-516580;
P10415:BCL2; NbExp=8; IntAct=EBI-526406, EBI-77694;
Q16548:BCL2A1; NbExp=5; IntAct=EBI-526406, EBI-1003550;
Q07440:Bcl2a1 (xeno); NbExp=2; IntAct=EBI-526406, EBI-707754;
Q07817:BCL2L1; NbExp=4; IntAct=EBI-526406, EBI-78035;
Q07817-1:BCL2L1; NbExp=10; IntAct=EBI-526406, EBI-287195;
Q9HD36:BCL2L10; NbExp=7; IntAct=EBI-526406, EBI-2126349;
Q92843:BCL2L2; NbExp=6; IntAct=EBI-526406, EBI-707714;
P68451:F1L (xeno); NbExp=4; IntAct=EBI-526406, EBI-7066119;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-526406, EBI-10178634;
Q07820:MCL1; NbExp=16; IntAct=EBI-526406, EBI-1003422;
P97287:Mcl1 (xeno); NbExp=7; IntAct=EBI-526406, EBI-707292;
P14174:MIF; NbExp=5; IntAct=EBI-526420, EBI-372712;
P03495:NS (xeno); NbExp=2; IntAct=EBI-526406, EBI-2548993;
P63244:RACK1; NbExp=2; IntAct=EBI-526406, EBI-296739;
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Note=Associated with
intracytoplasmic membranes. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform BimEL: Mitochondrion.
Note=Translocates from microtubules to motochondria on loss of
cell adherence.
-!- SUBCELLULAR LOCATION: Isoform BimL: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform BimS: Mitochondrion.
-!- SUBCELLULAR LOCATION: Isoform Bim-alpha1: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=20;
Name=BimEL; Synonyms=Bim(EL);
IsoId=O43521-1; Sequence=Displayed;
Name=BimL; Synonyms=Bim(L);
IsoId=O43521-2; Sequence=VSP_000535;
Name=BimS; Synonyms=BCL2-like 11 transcript variant 9, Bim(S);
IsoId=O43521-3; Sequence=VSP_035608;
Name=Bim-alpha1; Synonyms=BimABCD, Bim-ABCD;
IsoId=O43521-4; Sequence=VSP_035620;
Name=Bim-alpha2; Synonyms=BimACD, Bim-ACD;
IsoId=O43521-5; Sequence=VSP_000535, VSP_035620;
Name=Bim-alpha3; Synonyms=BCL2-like 11 transcript variant 10,
BimAD, Bim-AD;
IsoId=O43521-6; Sequence=VSP_035608, VSP_035620;
Name=Bim-alpha4;
IsoId=O43521-7; Sequence=VSP_035608, VSP_035618;
Name=Bim-alpha5;
IsoId=O43521-8; Sequence=VSP_035619;
Name=Bim-alpha6;
IsoId=O43521-9; Sequence=VSP_035608, VSP_035619;
Name=Bim-beta1;
IsoId=O43521-10; Sequence=VSP_035615, VSP_035616;
Name=Bim-beta2;
IsoId=O43521-11; Sequence=VSP_035614, VSP_035616;
Name=Bim-beta3;
IsoId=O43521-12; Sequence=VSP_035609;
Name=Bim-beta4;
IsoId=O43521-13; Sequence=VSP_035610, VSP_035611;
Name=Bim-beta5;
IsoId=O43521-14; Sequence=VSP_035613, VSP_035617;
Name=Bim-beta6;
IsoId=O43521-15; Sequence=VSP_000535, VSP_035614, VSP_035616;
Name=Bim-beta7;
IsoId=O43521-16; Sequence=VSP_000535, VSP_035613, VSP_035617;
Name=Bim-gamma;
IsoId=O43521-17; Sequence=VSP_000535, VSP_035612;
Name=BimABC; Synonyms=Bim-ABC;
IsoId=O43521-18; Sequence=VSP_000535, VSP_042866;
Name=BimAC; Synonyms=Bim-AC;
IsoId=O43521-19; Sequence=VSP_042866;
Name=BimA; Synonyms=Bim-A;
IsoId=O43521-20; Sequence=VSP_042865;
-!- TISSUE SPECIFICITY: Isoform BimEL, isoform BimL and isoform BimS
are the predominant isoforms and are widely expressed with tissue-
specific variation. Isoform Bim-gamma is most abundantly expressed
in small intestine and colon, and in lower levels in spleen,
prostate, testis, heart, liver and kidney.
{ECO:0000269|PubMed:12019181}.
-!- INDUCTION: By ER stress in a DDIT3/CHOP-dependent manner.
{ECO:0000269|PubMed:22761832}.
-!- DOMAIN: The BH3 motif is required for interaction with Bcl-2
proteins and cytotoxicity. {ECO:0000250|UniProtKB:O54918}.
-!- PTM: Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction
with TRIM2 and polyubiquitination, followed by proteasomal
degradation (PubMed:15486195, PubMed:21478148). Deubiquitination
catalyzed by USP27X stabilizes the protein (By similarity).
{ECO:0000250|UniProtKB:O54918, ECO:0000269|PubMed:15486195,
ECO:0000269|PubMed:21478148}.
-!- PTM: Ubiquitination by TRIM2 following phosphorylation by
MAPK1/MAPK3 leads to proteasomal degradation. Conversely,
deubiquitination catalyzed by USP27X stabilizes the protein.
{ECO:0000250|UniProtKB:O54918}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCL2L11ID772ch2q13.html";
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EMBL; AF032457; AAC39593.1; -; mRNA.
EMBL; AF032458; AAC39594.1; -; mRNA.
EMBL; AB071195; BAB78589.1; -; mRNA.
EMBL; AB071196; BAB78590.1; -; mRNA.
EMBL; AB071197; BAB78591.1; -; mRNA.
EMBL; AB071198; BAB78592.1; -; mRNA.
EMBL; AB071199; BAB78593.1; -; mRNA.
EMBL; AB071200; BAB78594.1; -; mRNA.
EMBL; AY352518; AAQ62569.1; -; mRNA.
EMBL; AY305714; AAQ82546.1; -; mRNA.
EMBL; AY305715; AAQ82547.1; -; mRNA.
EMBL; AY423441; AAQ99148.1; -; mRNA.
EMBL; AY423442; AAQ99149.1; -; mRNA.
EMBL; AY423443; AAQ99150.1; -; mRNA.
EMBL; AY428962; AAR06908.1; -; mRNA.
EMBL; DQ849200; ABI13589.1; -; mRNA.
EMBL; DQ849201; ABI13590.1; -; mRNA.
EMBL; DQ849202; ABI13591.1; -; mRNA.
EMBL; AK290377; BAF83066.1; -; mRNA.
EMBL; AK291269; BAF83958.1; -; mRNA.
EMBL; AC096670; AAY14797.1; -; Genomic_DNA.
EMBL; CH471237; EAW50365.1; -; Genomic_DNA.
EMBL; CH471237; EAW50367.1; -; Genomic_DNA.
EMBL; CH471237; EAW50369.1; -; Genomic_DNA.
EMBL; CH471237; EAW50370.1; -; Genomic_DNA.
EMBL; CH471237; EAW50371.1; -; Genomic_DNA.
EMBL; CH471237; EAW50372.1; -; Genomic_DNA.
EMBL; CH471237; EAW50373.1; -; Genomic_DNA.
EMBL; CH471237; EAW50374.1; -; Genomic_DNA.
EMBL; BC033694; AAH33694.1; -; mRNA.
CCDS; CCDS2089.1; -. [O43521-1]
CCDS; CCDS2092.1; -. [O43521-17]
CCDS; CCDS42731.1; -. [O43521-2]
CCDS; CCDS56131.1; -. [O43521-16]
CCDS; CCDS56132.1; -. [O43521-7]
CCDS; CCDS56133.1; -. [O43521-9]
CCDS; CCDS56134.1; -. [O43521-10]
CCDS; CCDS56135.1; -. [O43521-8]
CCDS; CCDS56136.1; -. [O43521-14]
CCDS; CCDS74560.1; -. [O43521-4]
CCDS; CCDS74561.1; -. [O43521-11]
RefSeq; NP_001191035.1; NM_001204106.1. [O43521-3]
RefSeq; NP_001191036.1; NM_001204107.1. [O43521-7]
RefSeq; NP_001191037.1; NM_001204108.1. [O43521-8]
RefSeq; NP_001191038.1; NM_001204109.1. [O43521-14]
RefSeq; NP_001191039.1; NM_001204110.1. [O43521-9]
RefSeq; NP_001191040.1; NM_001204111.1. [O43521-15]
RefSeq; NP_001191041.1; NM_001204112.1. [O43521-16]
RefSeq; NP_001191042.1; NM_001204113.1.
RefSeq; NP_006529.1; NM_006538.4. [O43521-2]
RefSeq; NP_619527.1; NM_138621.4. [O43521-1]
RefSeq; NP_619528.1; NM_138622.3. [O43521-4]
RefSeq; NP_619529.1; NM_138623.3. [O43521-5]
RefSeq; NP_619530.1; NM_138624.3. [O43521-10]
RefSeq; NP_619531.1; NM_138625.3.
RefSeq; NP_619532.1; NM_138626.3. [O43521-11]
RefSeq; NP_619533.1; NM_138627.3.
RefSeq; NP_996885.1; NM_207002.3. [O43521-17]
RefSeq; NP_996886.1; NM_207003.2. [O43521-6]
UniGene; Hs.469658; -.
UniGene; Hs.737004; -.
PDB; 1F95; NMR; -; C/D=108-116.
PDB; 2K7W; NMR; -; B=145-164.
PDB; 2NL9; X-ray; 1.55 A; B=141-166.
PDB; 2V6Q; X-ray; 2.70 A; B=141-166.
PDB; 2VM6; X-ray; 2.20 A; B=141-165.
PDB; 2WH6; X-ray; 1.50 A; B=141-166.
PDB; 2YQ6; X-ray; 1.80 A; B=147-164.
PDB; 2YQ7; X-ray; 1.90 A; B=147-164.
PDB; 3D7V; X-ray; 2.03 A; B=141-166.
PDB; 3FDL; X-ray; 1.78 A; B=141-166.
PDB; 3IO8; X-ray; 2.30 A; B/D=141-166.
PDB; 3IO9; X-ray; 2.40 A; B=141-166.
PDB; 3KJ0; X-ray; 1.70 A; B=143-165.
PDB; 3KJ1; X-ray; 1.94 A; B=143-163.
PDB; 3KJ2; X-ray; 2.35 A; B=143-163.
PDB; 4A1U; X-ray; 1.54 A; B=146-163.
PDB; 4A1W; X-ray; 2.50 A; P/Q/R/S=146-163.
PDB; 4B4S; X-ray; 1.90 A; B=141-166.
PDB; 4D2M; X-ray; 2.10 A; B/D=141-166.
PDB; 4QVF; X-ray; 1.53 A; B=141-166.
PDB; 4UF3; X-ray; 2.70 A; B=141-166.
PDB; 4YJ4; X-ray; 2.10 A; B=146-165.
PDB; 4ZIE; X-ray; 1.80 A; C=141-166.
PDB; 4ZIF; X-ray; 2.40 A; B=141-160.
PDB; 4ZIH; X-ray; 2.50 A; B=141-160.
PDB; 5AGW; X-ray; 2.69 A; C/D=146-166.
PDB; 5AGX; X-ray; 2.24 A; C/D=146-166.
PDB; 5C3G; X-ray; 2.45 A; B=146-166.
PDBsum; 1F95; -.
PDBsum; 2K7W; -.
PDBsum; 2NL9; -.
PDBsum; 2V6Q; -.
PDBsum; 2VM6; -.
PDBsum; 2WH6; -.
PDBsum; 2YQ6; -.
PDBsum; 2YQ7; -.
PDBsum; 3D7V; -.
PDBsum; 3FDL; -.
PDBsum; 3IO8; -.
PDBsum; 3IO9; -.
PDBsum; 3KJ0; -.
PDBsum; 3KJ1; -.
PDBsum; 3KJ2; -.
PDBsum; 4A1U; -.
PDBsum; 4A1W; -.
PDBsum; 4B4S; -.
PDBsum; 4D2M; -.
PDBsum; 4QVF; -.
PDBsum; 4UF3; -.
PDBsum; 4YJ4; -.
PDBsum; 4ZIE; -.
PDBsum; 4ZIF; -.
PDBsum; 4ZIH; -.
PDBsum; 5AGW; -.
PDBsum; 5AGX; -.
PDBsum; 5C3G; -.
ProteinModelPortal; O43521; -.
SMR; O43521; -.
BioGrid; 115335; 58.
CORUM; O43521; -.
DIP; DIP-29185N; -.
ELM; O43521; -.
IntAct; O43521; 39.
MINT; MINT-1664421; -.
STRING; 9606.ENSP00000376943; -.
BindingDB; O43521; -.
ChEMBL; CHEMBL5777; -.
TCDB; 8.A.69.1.1; the pro-apoptotic bcl-2-family protein bim (bim) family.
iPTMnet; O43521; -.
PhosphoSitePlus; O43521; -.
BioMuta; BCL2L11; -.
MaxQB; O43521; -.
PaxDb; O43521; -.
PeptideAtlas; O43521; -.
PRIDE; O43521; -.
DNASU; 10018; -.
Ensembl; ENST00000308659; ENSP00000309226; ENSG00000153094. [O43521-2]
Ensembl; ENST00000337565; ENSP00000338374; ENSG00000153094. [O43521-17]
Ensembl; ENST00000393256; ENSP00000376943; ENSG00000153094. [O43521-1]
Ensembl; ENST00000405953; ENSP00000384641; ENSG00000153094. [O43521-17]
Ensembl; ENST00000415458; ENSP00000393781; ENSG00000153094. [O43521-16]
Ensembl; ENST00000431217; ENSP00000394640; ENSG00000153094. [O43521-10]
Ensembl; ENST00000433098; ENSP00000401662; ENSG00000153094. [O43521-5]
Ensembl; ENST00000436733; ENSP00000403727; ENSG00000153094. [O43521-14]
Ensembl; ENST00000437029; ENSP00000412892; ENSG00000153094. [O43521-8]
Ensembl; ENST00000439718; ENSP00000411137; ENSG00000153094. [O43521-7]
Ensembl; ENST00000452231; ENSP00000391292; ENSG00000153094. [O43521-9]
Ensembl; ENST00000610735; ENSP00000481030; ENSG00000153094. [O43521-14]
Ensembl; ENST00000615946; ENSP00000481423; ENSG00000153094. [O43521-7]
Ensembl; ENST00000619294; ENSP00000479714; ENSG00000153094. [O43521-10]
Ensembl; ENST00000620862; ENSP00000478133; ENSG00000153094. [O43521-5]
Ensembl; ENST00000621302; ENSP00000481652; ENSG00000153094. [O43521-4]
Ensembl; ENST00000622509; ENSP00000482175; ENSG00000153094. [O43521-8]
Ensembl; ENST00000622612; ENSP00000484360; ENSG00000153094. [O43521-11]
Ensembl; ENST00000639340; ENSP00000491154; ENSG00000153094. [O43521-16]
Ensembl; ENST00000640419; ENSP00000491422; ENSG00000153094. [O43521-9]
GeneID; 10018; -.
KEGG; hsa:10018; -.
UCSC; uc002tgt.2; human. [O43521-1]
CTD; 10018; -.
DisGeNET; 10018; -.
EuPathDB; HostDB:ENSG00000153094.21; -.
GeneCards; BCL2L11; -.
HGNC; HGNC:994; BCL2L11.
HPA; CAB026332; -.
MIM; 603827; gene.
neXtProt; NX_O43521; -.
OpenTargets; ENSG00000153094; -.
PharmGKB; PA25305; -.
eggNOG; ENOG410IZKS; Eukaryota.
eggNOG; ENOG410Y8GB; LUCA.
GeneTree; ENSGT00390000003178; -.
InParanoid; O43521; -.
KO; K16341; -.
OMA; AEDHPQM; -.
OrthoDB; EOG091G0XD3; -.
PhylomeDB; O43521; -.
TreeFam; TF335898; -.
Reactome; R-HSA-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-8952158; RUNX3 regulates BCL2L11 (BIM) transcription.
SIGNOR; O43521; -.
ChiTaRS; BCL2L11; human.
EvolutionaryTrace; O43521; -.
GeneWiki; BCL2L11; -.
GenomeRNAi; 10018; -.
PMAP-CutDB; O43521; -.
PRO; PR:O43521; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000153094; -.
ExpressionAtlas; O43521; baseline and differential.
Genevisible; O43521; HS.
GO; GO:0097136; C:Bcl-2 family protein complex; IEA:Ensembl.
GO; GO:0097141; C:BIM-BCL-2 complex; IDA:UniProtKB.
GO; GO:0097140; C:BIM-BCL-xl complex; IDA:UniProtKB.
GO; GO:0005868; C:cytoplasmic dynein complex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
GO; GO:0043583; P:ear development; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IEA:Ensembl.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0032464; P:positive regulation of protein homooligomerization; IDA:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0035148; P:tube formation; IEA:Ensembl.
InterPro; IPR014771; Apoptosis_Bim_N.
InterPro; IPR017288; Bcl-2-like_11.
InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
Pfam; PF08945; Bclx_interact; 1.
Pfam; PF06773; Bim_N; 1.
PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
Ubl conjugation.
CHAIN 1 198 Bcl-2-like protein 11.
/FTId=PRO_0000143109.
MOTIF 148 162 BH3.
MOD_RES 69 69 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:15486195}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:O88498}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:O88498}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 42 166 Missing (in isoform BimA).
{ECO:0000303|PubMed:11997495}.
/FTId=VSP_042865.
VAR_SEQ 42 131 Missing (in isoform BimS, isoform Bim-
alpha3, isoform Bim-alpha6 and isoform
Bim-alpha4).
{ECO:0000303|PubMed:11997495,
ECO:0000303|PubMed:15147734,
ECO:0000303|PubMed:17503221}.
/FTId=VSP_035608.
VAR_SEQ 42 101 Missing (in isoform BimABC, isoform BimL,
isoform Bim-alpha2, isoform Bim-gamma,
isoform Bim-beta6 and isoform Bim-beta7).
{ECO:0000303|PubMed:11734221,
ECO:0000303|PubMed:11997495,
ECO:0000303|PubMed:12019181,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17503221,
ECO:0000303|PubMed:9430630}.
/FTId=VSP_000535.
VAR_SEQ 42 75 GNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFAT -> VSL
CHPGWSALVRSWLTATSNSQVQAVLLPQPPK (in
isoform Bim-beta3).
{ECO:0000303|PubMed:11734221}.
/FTId=VSP_035609.
VAR_SEQ 43 44 NP -> IF (in isoform Bim-beta4).
{ECO:0000303|PubMed:11734221}.
/FTId=VSP_035610.
VAR_SEQ 45 198 Missing (in isoform Bim-beta4).
{ECO:0000303|PubMed:11734221}.
/FTId=VSP_035611.
VAR_SEQ 132 198 ASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNY
QAAEDHPRMVILRLLRYIVRLVWRMH -> VVILEDIGDLS
LCFGFIFTGLDLYGHHHSQDTEQLNHKDFS (in
isoform Bim-gamma).
{ECO:0000303|PubMed:12019181}.
/FTId=VSP_035612.
VAR_SEQ 132 166 Missing (in isoform BimAC and isoform
BimABC). {ECO:0000303|PubMed:11997495}.
/FTId=VSP_042866.
VAR_SEQ 132 140 ASMRQAEPA -> VREIEEVVV (in isoform Bim-
beta5 and isoform Bim-beta7).
{ECO:0000303|PubMed:17503221}.
/FTId=VSP_035613.
VAR_SEQ 132 135 ASMR -> GIFE (in isoform Bim-beta2 and
isoform Bim-beta6).
{ECO:0000303|PubMed:11734221,
ECO:0000303|PubMed:17503221}.
/FTId=VSP_035614.
VAR_SEQ 133 135 SMR -> NWD (in isoform Bim-beta1).
{ECO:0000303|PubMed:11734221}.
/FTId=VSP_035615.
VAR_SEQ 136 198 Missing (in isoform Bim-beta1, isoform
Bim-beta2 and isoform Bim-beta6).
{ECO:0000303|PubMed:11734221,
ECO:0000303|PubMed:17503221}.
/FTId=VSP_035616.
VAR_SEQ 141 198 Missing (in isoform Bim-beta5 and isoform
Bim-beta7).
{ECO:0000303|PubMed:17503221}.
/FTId=VSP_035617.
VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LEK
(in isoform Bim-alpha1, isoform Bim-
alpha2 and isoform Bim-alpha3).
{ECO:0000303|PubMed:11734221,
ECO:0000303|PubMed:11997495,
ECO:0000303|PubMed:15147734,
ECO:0000303|PubMed:17503221}.
/FTId=VSP_035620.
VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> LAKLL
ASST (in isoform Bim-alpha4).
{ECO:0000303|PubMed:17503221}.
/FTId=VSP_035618.
VAR_SEQ 167 198 VFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH -> MPLPP
D (in isoform Bim-alpha5 and isoform Bim-
alpha6). {ECO:0000303|PubMed:17503221}.
/FTId=VSP_035619.
MUTAGEN 156 156 G->A: Retains the ability to induce
apoptosis. Abolishes interaction with
BAX; in isoform Bim-alpha3 and isoform
BimS. No effect on interaction with BCL2.
{ECO:0000269|PubMed:11997495,
ECO:0000269|PubMed:17289999}.
MUTAGEN 156 156 G->E: Abolishes induction of apoptosis.
Abolishes interaction with BAX and BCL2;
in isoform Bim-alpha3 and isoform BimS.
Loses the ability to induce the
conformationally active form of BAX.
{ECO:0000269|PubMed:11997495,
ECO:0000269|PubMed:17289999}.
MUTAGEN 160 160 N->A: Retains the ability to induce
apoptosis. Abolishes interaction with
BCL2; in isoform Bim-alpha3 and isoform
BimS. No effect on interaction with BAX.
{ECO:0000269|PubMed:11997495}.
CONFLICT 33 33 P -> L (in Ref. 7; BAF83066).
{ECO:0000305}.
STRAND 112 115 {ECO:0000244|PDB:1F95}.
HELIX 143 159 {ECO:0000244|PDB:2WH6}.
TURN 160 163 {ECO:0000244|PDB:5AGX}.
SEQUENCE 198 AA; 22171 MW; D75735E469CA6997 CRC64;
MAKQPSDVSS ECDREGRQLQ PAERPPQLRP GAPTSLQTEP QGNPEGNHGG EGDSCPHGSP
QGPLAPPASP GPFATRSPLF IFMRRSSLLS RSSSGYFSFD TDRSPAPMSC DKSTQTPSPP
CQAFNHYLSA MASMRQAEPA DMRPEIWIAQ ELRRIGDEFN AYYARRVFLN NYQAAEDHPR
MVILRLLRYI VRLVWRMH


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