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

Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)

 B2CL1_RAT               Reviewed;         233 AA.
P53563; P70613; P70614; Q52KS0; Q62678; Q62836; Q64087; Q64128;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
27-SEP-2017, entry version 167.
RecName: Full=Bcl-2-like protein 1;
Short=Bcl2-L-1;
AltName: Full=Apoptosis regulator Bcl-X;
Name=Bcl2l1; Synonyms=Bclx, Blc2l;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BCL-X(L) AND BCL-X(S)).
TISSUE=Brain;
Michaelidis T.M.;
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE (ISOFORM BCL-X(L)).
TISSUE=Brain;
Wesselingh S.L., David G.L., Choi S., Veliuona M., Hardwick J.M.;
"Cloning and expression of rat bcl-x in cultured neurons.";
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND
FUNCTION.
TISSUE=Thymus;
PubMed=8662675; DOI=10.1074/jbc.271.22.13258;
Shiraiwa N., Inohara N., Okada S., Yuzaki M., Shoji S., Ohta S.;
"An additional form of rat Bcl-x, Bcl-xbeta, generated by an unspliced
RNA, promotes apoptosis in promyeloid cells.";
J. Biol. Chem. 271:13258-13265(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(S)), AND
FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Ovary;
PubMed=7828536; DOI=10.1210/endo.136.1.7828536;
Tilly J.L., Tilly K.I., Kenton M.L., Johnson A.L.;
"Expression of members of the Bcl-2 gene family in the immature rat
ovary: equine chorionic gonadotropin-mediated inhibition of granulosa
cell apoptosis is associated with decreased Bax and constitutive Bcl-2
and Bcl-xlong messenger ribonucleic acid levels.";
Endocrinology 136:232-241(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
TISSUE=Brain;
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).
[6]
FUNCTION IN SYNAPTIC VESICLE REGULATION, AND INTERACTION WITH DNM1L.
PubMed=18250306; DOI=10.1073/pnas.0711647105;
Li H., Chen Y., Jones A.F., Sanger R.H., Collis L.P., Flannery R.,
McNay E.C., Yu T., Schwarzenbacher R., Bossy B., Bossy-Wetzel E.,
Bennett M.V., Pypaert M., Hickman J.A., Smith P.J., Hardwick J.M.,
Jonas E.A.;
"Bcl-xL induces Drp1-dependent synapse formation in cultured
hippocampal neurons.";
Proc. Natl. Acad. Sci. U.S.A. 105:2169-2174(2008).
[7]
FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH ATP5A1 AND
ATP5B, AND SUBCELLULAR LOCATION.
PubMed=21926988; DOI=10.1038/ncb2330;
Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S.,
Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M.,
Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J.,
Hardwick J.M., Jonas E.A.;
"Bcl-xL regulates metabolic efficiency of neurons through interaction
with the mitochondrial F1FO ATP synthase.";
Nat. Cell Biol. 13:1224-1233(2011).
[8]
FUNCTION IN SYNAPTIC VESICLE REGULATION, SUBCELLULAR LOCATION, AND
INTERACTION WITH CLTA; DNM1L AND MFF.
PubMed=23792689; DOI=10.1038/ncb2791;
Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
Morrison R.S., Jonas E.A.;
"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
during endocytosis.";
Nat. Cell Biol. 15:773-785(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=9346936; DOI=10.1074/jbc.272.44.27886;
Aritomi M., Kunishima N., Inohara N., Ishibashi Y., Ohta S.,
Morikawa K.;
"Crystal structure of rat Bcl-xL. Implications for the function of the
Bcl-2 protein family.";
J. Biol. Chem. 272:27886-27892(1997).
-!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
caspases. Appears to regulate cell death by blocking the voltage-
dependent anion channel (VDAC) by binding to it and preventing the
release of the caspase activator, CYC1, from the mitochondrial
membrane. Also acts as a regulator of G2 checkpoint and
progression to cytokinesis during mitosis.
-!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity,
including neurotransmitter release and recovery, number of axonal
mitochondria as well as size and number of synaptic vesicle
clusters. During synaptic stimulation, increases ATP availability
from mitochondria through regulation of mitochondrial membrane ATP
synthase F(1)F(0) activity and regulates endocytic vesicle
retrieval in hippocampal neurons through association with DMN1L
and stimulation of its GTPase activity in synaptic vesicles. May
attenuate inflammation impairing NLRP1-inflammasome activation,
hence CASP1 activation and IL1B release (By similarity).
{ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:18250306,
ECO:0000269|PubMed:21926988, ECO:0000269|PubMed:23792689,
ECO:0000269|PubMed:7828536, ECO:0000269|PubMed:8662675}.
-!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
-!- SUBUNIT: Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX,
BAK or BCL2. Heterodimerization with BAX does not seem to be
required for anti-apoptotic activity. Interacts with BCL2L11.
Interacts with BAD. Isoform Bcl-X(L) interacts with SIVA1 isoform
1; the interaction inhibits the anti-apoptotic activity. Interacts
with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with IKZF3.
Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP.
Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts
the interaction with p53/TP53. Isoform Bcl-X(L) interacts with
DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a
complex in synaptic vesicles that also contains clathrin and MFF.
Interacts with ATP5A and ATP5B; the interactions mediate the
association of isoform Bcl-X(L) with the mitochondrial membrane
ATP synthase F(1)F(0) ATP synthase. Interacts with VDAC1 (By
similarity). Isoform Bcl-X(L) interacts (via the loop between
motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with
NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts
with BCL2L11 (via BH3) (By similarity).
{ECO:0000250|UniProtKB:Q07817, ECO:0000250|UniProtKB:Q64373,
ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:21926988,
ECO:0000269|PubMed:23792689}.
-!- INTERACTION:
O35303:Dnm1l; NbExp=2; IntAct=EBI-287204, EBI-1767447;
-!- SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion inner
membrane. Mitochondrion outer membrane. Mitochondrion matrix.
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane.
Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Nucleus membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Note=Localizes to the centrosome
when phosphorylated at Ser-49 (By similarity). After neuronal
stimulation, translocates from cytosol to synaptic vesicle and
mitochondrion membrane in a calmodulin-dependent manner.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Bcl-X(L); Synonyms=Bcl-xL;
IsoId=P53563-1; Sequence=Displayed;
Name=Bcl-X(S); Synonyms=Bcl-xS;
IsoId=P53563-2; Sequence=VSP_000520;
Name=Bcl-X(beta);
IsoId=P53563-3; Sequence=VSP_000521;
-!- TISSUE SPECIFICITY: Expressed in most tissues. Bcl-X(beta) is
specifically expressed in cerebellum, heart, and thymus. In the
ovary, the predominant form is Bcl-X(L), with a small but
detectable level of Bcl-X(S).
-!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The
BH1 and BH2 motifs are required for both heterodimerization with
other Bcl-2 family members and for repression of cell death.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic activity
(By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is
partial in normal mitotic cells, but complete in G2-arrested cells
upon DNA-damage, thus promoting subsequent apoptosis probably by
triggering caspases-mediated proteolysis. Phosphorylated by PLK3,
leading to regulate the G2 checkpoint and progression to
cytokinesis during mitosis. Phosphorylation at Ser-49 appears
during the S phase and G2, disappears rapidly in early mitosis
during prometaphase, metaphase and early anaphase, and re-appears
during telophase and cytokinesis (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC60701.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAC60702.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X82537; CAA57886.1; -; Genomic_DNA.
EMBL; X82537; CAA57887.1; -; Genomic_DNA.
EMBL; U10579; AAA19257.1; -; Unassigned_DNA.
EMBL; U72350; AAB17353.1; -; mRNA.
EMBL; U72349; AAB17352.1; -; mRNA.
EMBL; U34963; AAA77686.1; -; mRNA.
EMBL; S76513; AAC60701.2; ALT_INIT; mRNA.
EMBL; S78284; AAC60702.1; ALT_INIT; mRNA.
EMBL; BC094213; AAH94213.1; -; mRNA.
PIR; I67431; I67431.
PIR; I67435; I67435.
PIR; S51761; S51761.
RefSeq; NP_001028842.1; NM_001033670.1. [P53563-1]
RefSeq; NP_001028843.1; NM_001033671.1. [P53563-2]
RefSeq; NP_113723.2; NM_031535.2.
RefSeq; XP_006235327.1; XM_006235265.3. [P53563-1]
UniGene; Rn.10323; -.
PDB; 1AF3; X-ray; 2.50 A; A=1-196.
PDB; 4QNQ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-233.
PDBsum; 1AF3; -.
PDBsum; 4QNQ; -.
DisProt; DP00449; -.
ProteinModelPortal; P53563; -.
SMR; P53563; -.
BioGrid; 246998; 5.
CORUM; P53563; -.
DIP; DIP-29698N; -.
IntAct; P53563; 2.
STRING; 10116.ENSRNOP00000043542; -.
ChEMBL; CHEMBL1075182; -.
iPTMnet; P53563; -.
PhosphoSitePlus; P53563; -.
SwissPalm; P53563; -.
PaxDb; P53563; -.
PRIDE; P53563; -.
Ensembl; ENSRNOT00000010762; ENSRNOP00000010762; ENSRNOG00000007946. [P53563-1]
GeneID; 24888; -.
KEGG; rno:24888; -.
UCSC; RGD:2200; rat. [P53563-1]
CTD; 598; -.
RGD; 2200; Bcl2l1.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
GeneTree; ENSGT00530000062935; -.
InParanoid; P53563; -.
KO; K04570; -.
OMA; NGSPSWH; -.
PhylomeDB; P53563; -.
EvolutionaryTrace; P53563; -.
PRO; PR:P53563; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000007946; -.
ExpressionAtlas; P53563; baseline and differential.
Genevisible; P53563; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005740; C:mitochondrial envelope; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; IDA:CAFA.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051400; F:BH domain binding; IPI:RGD.
GO; GO:0030276; F:clathrin binding; IPI:CAFA.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:RGD.
GO; GO:0051020; F:GTPase binding; IPI:CAFA.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEP:RGD.
GO; GO:1905218; P:cellular response to astaxanthin; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0036018; P:cellular response to erythropoietin; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
GO; GO:1904579; P:cellular response to thapsigargin; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:CAFA.
GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:CAFA.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:CAFA.
GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
GO; GO:1900452; P:regulation of long term synaptic depression; IMP:CAFA.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0036017; P:response to erythropoietin; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0002931; P:response to ischemia; IDA:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:CAFA.
InterPro; IPR013279; Apop_reg_BclX.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR004725; Bcl2/BclX.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR003093; Bcl2_BH4.
InterPro; IPR020731; Bcl2_BH4_motif_CS.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF61; PTHR11256:SF61; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01864; APOPREGBCLX.
PRINTS; PR01862; BCL2FAMILY.
SMART; SM00265; BH4; 1.
SUPFAM; SSF56854; SSF56854; 1.
TIGRFAMs; TIGR00865; bcl-2; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
PROSITE; PS01260; BH4_1; 1.
PROSITE; PS50063; BH4_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell junction;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Endocytosis; Membrane; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 233 Bcl-2-like protein 1.
/FTId=PRO_0000143065.
TRANSMEM 210 226 Helical. {ECO:0000255}.
MOTIF 4 24 BH4.
MOTIF 86 100 BH3.
MOTIF 129 148 BH1.
MOTIF 180 195 BH2.
MOD_RES 49 49 Phosphoserine; by PLK3.
{ECO:0000250|UniProtKB:Q07817}.
MOD_RES 62 62 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q07817}.
VAR_SEQ 126 188 Missing (in isoform Bcl-X(S)).
{ECO:0000305}.
/FTId=VSP_000520.
VAR_SEQ 189 233 DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSL
FSRK -> VRTTPLVCPPLVCLSSVEIPNCPFWSPGMVVED
IDYSGDIPGLL (in isoform Bcl-X(beta)).
{ECO:0000305}.
/FTId=VSP_000521.
CONFLICT 6 6 R -> Q (in Ref. 1; CAA57886/CAA57887).
{ECO:0000305}.
CONFLICT 12 12 F -> S (in Ref. 2; AAA19257).
{ECO:0000305}.
CONFLICT 64 64 A -> E (in Ref. 2; AAA19257).
{ECO:0000305}.
CONFLICT 81 81 I -> L (in Ref. 4; AAA77686/AAC60701/
AAC60702). {ECO:0000305}.
CONFLICT 119 119 A -> V (in Ref. 4; AAA77686/AAC60701/
AAC60702). {ECO:0000305}.
CONFLICT 143 144 FF -> SS (in Ref. 4; AAA77686/AAC60701).
{ECO:0000305}.
CONFLICT 199 199 A -> T (in Ref. 4; AAA77686/AAC60701/
AAC60702). {ECO:0000305}.
CONFLICT 201 201 A -> P (in Ref. 4; AAA77686/AAC60701/
AAC60702). {ECO:0000305}.
HELIX 2 19 {ECO:0000244|PDB:4QNQ}.
TURN 25 28 {ECO:0000244|PDB:1AF3}.
HELIX 82 100 {ECO:0000244|PDB:4QNQ}.
HELIX 102 111 {ECO:0000244|PDB:4QNQ}.
TURN 116 118 {ECO:0000244|PDB:4QNQ}.
HELIX 119 130 {ECO:0000244|PDB:4QNQ}.
TURN 131 133 {ECO:0000244|PDB:4QNQ}.
HELIX 137 156 {ECO:0000244|PDB:4QNQ}.
HELIX 162 177 {ECO:0000244|PDB:4QNQ}.
HELIX 179 184 {ECO:0000244|PDB:4QNQ}.
HELIX 187 196 {ECO:0000244|PDB:4QNQ}.
SEQUENCE 233 AA; 26158 MW; 2B62B6C63864BC8F CRC64;
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA INGNPSWHLA
DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP
WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK


Related products :

Catalog number Product name Quantity
U1343h CLIA Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
E1343h ELISA kit Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
E1343h ELISA Apoptosis regulator BAX,BAX,BCL2L4,Bcl2-L-4,Bcl-2-like protein 4,Homo sapiens,Human 96T
CSB-EL002611BO Bovine Apoptosis regulator Bcl-2(BCL2) ELISA kit 96T
CSB-EL002611CH Chicken Apoptosis regulator Bcl-2(BCL2) ELISA kit 96T
U0778b CLIA Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
CSB-EL002611BO Bovine Apoptosis regulator Bcl-2(BCL2) ELISA kit SpeciesBovine 96T
CSB-EL002611CH Chicken Apoptosis regulator Bcl-2(BCL2) ELISA kit SpeciesChicken 96T
E0778b ELISA kit Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
U0778m CLIA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
E0778m ELISA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
E0778r ELISA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778m ELISA kit Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Mouse,Mus musculus 96T
U0778r CLIA Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778r ELISA kit Apoptosis regulator Bcl-2,Bcl2,Bcl-2,Rat,Rattus norvegicus 96T
E0778b ELISA Apoptosis regulator Bcl-2,BCL2,Bos taurus,Bovine 96T
E0778b ELISA Kit FOR Apoptosis regulator Bcl-2; organism: Bovine; gene name: BCL2 96T
E0778h ELISA kit Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
U0778h CLIA Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
E0778h ELISA Apoptosis regulator Bcl-2,BCL2,Homo sapiens,Human 96T
GWB-E2C8B2 Apoptosis Regulator Bcl-2 (BCL2) Rabbit anti-Human Polyclonal (Thr56) Antibody
GWB-47C732 Apoptosis Regulator Bcl-2 (BCL2) Rabbit anti-Human Polyclonal (Ser70) Antibody
E0778c ELISA kit Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T
E0778c ELISA Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T
U0778c CLIA Apoptosis regulator Bcl-2,BCL2,BCL-2,Chicken,Gallus gallus 96T


 

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

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





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

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

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

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

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

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

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




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






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






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

GENTAUR Poland Sp. z o.o.


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

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

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